Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P22894

- MMP8_HUMAN

UniProt

P22894 - MMP8_HUMAN

Protein

Neutrophil collagenase

Gene

MMP8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Can degrade fibrillar type I, II, and III collagens.

    Catalytic activityi

    Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.

    Cofactori

    Binds 3 calcium ions per subunit.
    Binds 2 zinc ions per subunit.

    Enzyme regulationi

    Cannot be activated without removal of the activation peptide.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi91 – 911Zinc 2; in inhibited form
    Metal bindingi157 – 1571Calcium 1
    Metal bindingi167 – 1671Zinc 11 Publication
    Metal bindingi169 – 1691Zinc 11 Publication
    Metal bindingi174 – 1741Calcium 21 Publication
    Metal bindingi175 – 1751Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi177 – 1771Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi179 – 1791Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi182 – 1821Zinc 11 Publication
    Metal bindingi189 – 1891Calcium 1; via carbonyl oxygen
    Metal bindingi191 – 1911Calcium 1; via carbonyl oxygen
    Metal bindingi193 – 1931Calcium 1
    Metal bindingi195 – 1951Zinc 11 Publication
    Metal bindingi197 – 1971Calcium 21 Publication
    Metal bindingi200 – 2001Calcium 21 Publication
    Metal bindingi217 – 2171Zinc 2; catalytic1 Publication
    Active sitei218 – 2181
    Metal bindingi221 – 2211Zinc 2; catalytic1 Publication
    Metal bindingi227 – 2271Zinc 2; catalytic1 Publication
    Metal bindingi286 – 2861Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi378 – 3781Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi425 – 4251Calcium 3; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. serine-type endopeptidase activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. collagen catabolic process Source: Reactome
    2. extracellular matrix disassembly Source: Reactome
    3. extracellular matrix organization Source: Reactome
    4. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil collagenase (EC:3.4.24.34)
    Alternative name(s):
    Matrix metalloproteinase-8
    Short name:
    MMP-8
    PMNL collagenase
    Short name:
    PMNL-CL
    Gene namesi
    Name:MMP8
    Synonyms:CLG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7175. MMP8.

    Subcellular locationi

    Cytoplasmic granule. Secretedextracellular spaceextracellular matrix Curated
    Note: Stored in intracellular granules.

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30888.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20202 PublicationsAdd
    BLAST
    Propeptidei21 – 10080Activation peptidePRO_0000028744Add
    BLAST
    Chaini101 – 467367Neutrophil collagenasePRO_0000028745Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)Curated
    Glycosylationi73 – 731N-linked (GlcNAc...)Curated
    Glycosylationi112 – 1121N-linked (GlcNAc...)
    Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi279 ↔ 464Curated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP22894.
    PeptideAtlasiP22894.
    PRIDEiP22894.

    PTM databases

    PhosphoSiteiP22894.

    Miscellaneous databases

    PMAP-CutDBP22894.

    Expressioni

    Tissue specificityi

    Neutrophils.

    Gene expression databases

    ArrayExpressiP22894.
    BgeeiP22894.
    CleanExiHS_MMP8.
    GenevestigatoriP22894.

    Organism-specific databases

    HPAiHPA021221.
    HPA022935.

    Interactioni

    Protein-protein interaction databases

    BioGridi110460. 2 interactions.
    STRINGi9606.ENSP00000236826.

    Structurei

    Secondary structure

    1
    467
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi107 – 1093
    Beta strandi111 – 1177
    Beta strandi122 – 1243
    Helixi126 – 14116
    Beta strandi147 – 1504
    Beta strandi152 – 1543
    Beta strandi157 – 1637
    Beta strandi168 – 1703
    Beta strandi175 – 1784
    Beta strandi181 – 1833
    Beta strandi186 – 1883
    Turni189 – 1924
    Beta strandi194 – 1974
    Beta strandi203 – 2086
    Helixi211 – 22313
    Beta strandi236 – 2383
    Beta strandi244 – 2463
    Helixi251 – 26111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A85X-ray2.00A105-262[»]
    1A86X-ray2.00A105-262[»]
    1BZSX-ray1.70A99-262[»]
    1I73X-ray1.40A100-262[»]
    1I76X-ray1.20A100-262[»]
    1JANX-ray2.50A99-262[»]
    1JAOX-ray2.40A100-262[»]
    1JAPX-ray1.82A100-262[»]
    1JAQX-ray2.40A100-262[»]
    1JH1X-ray2.70A105-262[»]
    1JJ9X-ray2.00A100-262[»]
    1KBCX-ray1.80A/B99-262[»]
    1MMBX-ray2.10A100-262[»]
    1MNCX-ray2.10A101-263[»]
    1ZP5X-ray1.80A100-262[»]
    1ZS0X-ray1.56A100-262[»]
    1ZVXX-ray1.87A100-262[»]
    2OY2X-ray1.50A/F105-262[»]
    2OY4X-ray1.70A/F105-262[»]
    3DNGX-ray2.00A/B100-262[»]
    3DPEX-ray1.60A100-262[»]
    3DPFX-ray2.10A/B100-262[»]
    3TT4X-ray1.88A104-262[»]
    ProteinModelPortaliP22894.
    SMRiP22894. Positions 33-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22894.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati276 – 32550Hemopexin 1Add
    BLAST
    Repeati326 – 37247Hemopexin 2Add
    BLAST
    Repeati374 – 42047Hemopexin 3Add
    BLAST
    Repeati421 – 46444Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi89 – 968Cysteine switchBy similarity

    Domaini

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG258253.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiP22894.
    KOiK01402.
    OMAiYAFREPS.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP22894.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028709. MMP8.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF137. PTHR10201:SF137. 1 hit.
    PfamiPF00045. Hemopexin. 3 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22894-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSLKTLPFL LLLHVQISKA FPVSSKEKNT KTVQDYLEKF YQLPSNQYQS    50
    TRKNGTNVIV EKLKEMQRFF GLNVTGKPNE ETLDMMKKPR CGVPDSGGFM 100
    LTPGNPKWER TNLTYRIRNY TPQLSEAEVE RAIKDAFELW SVASPLIFTR 150
    ISQGEADINI AFYQRDHGDN SPFDGPNGIL AHAFQPGQGI GGDAHFDAEE 200
    TWTNTSANYN LFLVAAHEFG HSLGLAHSSD PGALMYPNYA FRETSNYSLP 250
    QDDIDGIQAI YGLSSNPIQP TGPSTPKPCD PSLTFDAITT LRGEILFFKD 300
    RYFWRRHPQL QRVEMNFISL FWPSLPTGIQ AAYEDFDRDL IFLFKGNQYW 350
    ALSGYDILQG YPKDISNYGF PSSVQAIDAA VFYRSKTYFF VNDQFWRYDN 400
    QRQFMEPGYP KSISGAFPGI ESKVDAVFQQ EHFFHVFSGP RYYAFDLIAQ 450
    RVTRVARGNK WLNCRYG 467
    Length:467
    Mass (Da):53,412
    Last modified:August 1, 1991 - v1
    Checksum:i4D4602A53AD7F8BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401F → I AA sequence (PubMed:2159879)Curated
    Sequence conflicti48 – 481Y → V AA sequence (PubMed:2159879)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31S → C.1 Publication
    Corresponds to variant rs17099450 [ dbSNP | Ensembl ].
    VAR_025036
    Natural varianti32 – 321T → I.2 Publications
    Corresponds to variant rs3765620 [ dbSNP | Ensembl ].
    VAR_025037
    Natural varianti87 – 871K → E.1 Publication
    Corresponds to variant rs1940475 [ dbSNP | Ensembl ].
    VAR_006730
    Natural varianti154 – 1541G → E.1 Publication
    Corresponds to variant rs35056226 [ dbSNP | Ensembl ].
    VAR_025038
    Natural varianti193 – 1931D → V.1 Publication
    Corresponds to variant rs34428739 [ dbSNP | Ensembl ].
    VAR_025039
    Natural varianti246 – 2461N → Y.1 Publication
    Corresponds to variant rs35243553 [ dbSNP | Ensembl ].
    VAR_025040
    Natural varianti436 – 4361V → A.1 Publication
    Corresponds to variant rs34009635 [ dbSNP | Ensembl ].
    VAR_025041
    Natural varianti460 – 4601K → T.1 Publication
    Corresponds to variant rs35866072 [ dbSNP | Ensembl ].
    VAR_025042

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05556 mRNA. Translation: AAA88021.1.
    DQ141306 Genomic DNA. Translation: AAZ38714.1.
    BC074988 mRNA. Translation: AAH74988.1.
    BC074989 mRNA. Translation: AAH74989.1.
    CCDSiCCDS8320.1.
    PIRiA37073. KCHUN.
    RefSeqiNP_002415.1. NM_002424.2.
    UniGeneiHs.161839.

    Genome annotation databases

    EnsembliENST00000236826; ENSP00000236826; ENSG00000118113.
    GeneIDi4317.
    KEGGihsa:4317.
    UCSCiuc001phe.2. human.

    Polymorphism databases

    DMDMi116862.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05556 mRNA. Translation: AAA88021.1 .
    DQ141306 Genomic DNA. Translation: AAZ38714.1 .
    BC074988 mRNA. Translation: AAH74988.1 .
    BC074989 mRNA. Translation: AAH74989.1 .
    CCDSi CCDS8320.1.
    PIRi A37073. KCHUN.
    RefSeqi NP_002415.1. NM_002424.2.
    UniGenei Hs.161839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A85 X-ray 2.00 A 105-262 [» ]
    1A86 X-ray 2.00 A 105-262 [» ]
    1BZS X-ray 1.70 A 99-262 [» ]
    1I73 X-ray 1.40 A 100-262 [» ]
    1I76 X-ray 1.20 A 100-262 [» ]
    1JAN X-ray 2.50 A 99-262 [» ]
    1JAO X-ray 2.40 A 100-262 [» ]
    1JAP X-ray 1.82 A 100-262 [» ]
    1JAQ X-ray 2.40 A 100-262 [» ]
    1JH1 X-ray 2.70 A 105-262 [» ]
    1JJ9 X-ray 2.00 A 100-262 [» ]
    1KBC X-ray 1.80 A/B 99-262 [» ]
    1MMB X-ray 2.10 A 100-262 [» ]
    1MNC X-ray 2.10 A 101-263 [» ]
    1ZP5 X-ray 1.80 A 100-262 [» ]
    1ZS0 X-ray 1.56 A 100-262 [» ]
    1ZVX X-ray 1.87 A 100-262 [» ]
    2OY2 X-ray 1.50 A/F 105-262 [» ]
    2OY4 X-ray 1.70 A/F 105-262 [» ]
    3DNG X-ray 2.00 A/B 100-262 [» ]
    3DPE X-ray 1.60 A 100-262 [» ]
    3DPF X-ray 2.10 A/B 100-262 [» ]
    3TT4 X-ray 1.88 A 104-262 [» ]
    ProteinModelPortali P22894.
    SMRi P22894. Positions 33-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110460. 2 interactions.
    STRINGi 9606.ENSP00000236826.

    Chemistry

    BindingDBi P22894.
    ChEMBLi CHEMBL2095216.
    GuidetoPHARMACOLOGYi 1632.

    Protein family/group databases

    MEROPSi M10.002.

    PTM databases

    PhosphoSitei P22894.

    Polymorphism databases

    DMDMi 116862.

    Proteomic databases

    PaxDbi P22894.
    PeptideAtlasi P22894.
    PRIDEi P22894.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000236826 ; ENSP00000236826 ; ENSG00000118113 .
    GeneIDi 4317.
    KEGGi hsa:4317.
    UCSCi uc001phe.2. human.

    Organism-specific databases

    CTDi 4317.
    GeneCardsi GC11M102617.
    HGNCi HGNC:7175. MMP8.
    HPAi HPA021221.
    HPA022935.
    MIMi 120355. gene.
    neXtProti NX_P22894.
    PharmGKBi PA30888.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258253.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi P22894.
    KOi K01402.
    OMAi YAFREPS.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P22894.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei P22894.
    GeneWikii MMP8.
    GenomeRNAii 4317.
    NextBioi 16985.
    PMAP-CutDB P22894.
    PROi P22894.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22894.
    Bgeei P22894.
    CleanExi HS_MMP8.
    Genevestigatori P22894.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028709. MMP8.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF137. PTHR10201:SF137. 1 hit.
    Pfami PF00045. Hemopexin. 3 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases."
      Hasty K.A., Pourmotabbed T.F., Goldberg G.I., Thompson J.P., Spinella D.G., Stevens R.M., Mainardi C.L.
      J. Biol. Chem. 265:11421-11424(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 314-337; 347-363 AND 424-441.
      Tissue: Neutrophil.
    2. NIEHS SNPs program
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-3; ILE-32; GLU-87; GLU-154; VAL-193; TYR-246; ALA-436 AND THR-460.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    4. "Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms."
      Knaeuper V., Kraemer S., Reinke H., Tschesche H.
      Eur. J. Biochem. 189:295-300(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-140, VARIANT ILE-32.
      Tissue: Neutrophil.
    5. "Mercurial activation of human polymorphonuclear leucocyte procollagenase."
      Blaeser J., Knaeuper V., Osthues A., Reinke H., Tschesche H.
      Eur. J. Biochem. 202:1223-1230(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-103.
      Tissue: Neutrophil.
    6. "Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase."
      Mallya S.K., Mookthiar K.A., Gao Y., Brew K., Dioszegi M., Birkedal-Hansen H., van Wart H.E.
      Biochemistry 29:10628-10634(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 85-120, CHARACTERIZATION.
      Tissue: Neutrophil.
    7. "Partial amino acid sequence of human PMN leukocyte procollagenase."
      Knaeuper V., Kraemer S., Reinke H., Tschesche H.
      Biol. Chem. Hoppe-Seyler 371:295-304(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    8. Erratum
      Knaeuper V., Kraemer S., Reinke H., Tschesche H.
      Biol. Chem. Hoppe-Seyler 371:733-733(1990) [PubMed] [Europe PMC] [Abstract]
    9. "Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism."
      Blaeser J., Triebel S., Reinke H., Tschesche H.
      FEBS Lett. 313:59-61(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CYSTEINE-SWITCH MECHANISM.
      Tissue: Neutrophil.
    10. "The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity."
      Bode W., Reinemer P., Huber R., Klein T., Schnierer S., Tschesche H.
      EMBO J. 13:1263-1269(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-262.
    11. "Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study."
      Reinemer P., Grams F., Huber R., Kleine T., Schnierer S., Piper M., Tschesche H., Bode W.
      FEBS Lett. 338:227-233(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-262.
    12. "Structure of human neutrophil collagenase reveals large S1' specificity pocket."
      Stams T., Spurlino J.C., Smith D.L., Wahl R.C., Ho T.F., Qoronfleh M.W., Banks T.M., Rubin B.
      Nat. Struct. Biol. 1:119-123(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 100-262.
    13. "1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile."
      Betz M., Huxley P., Davies S.J., Mushtaq Y., Pieper M., Tschesche H., Bode W., Gomis-Rueth F.-X.
      Eur. J. Biochem. 247:356-363(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 100-262.
    14. "Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data."
      Brandstetter H., Engh R.A., von Roedern E.G., Moroder L., Huber R., Bode W., Grams F.
      Protein Sci. 7:1303-1309(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-262.

    Entry informationi

    Entry nameiMMP8_HUMAN
    AccessioniPrimary (citable) accession number: P22894
    Secondary accession number(s): Q45F99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3