Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neutrophil collagenase

Gene

MMP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 3 Ca2+ ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ 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

  • calcium ion binding Source: InterPro
  • metalloendopeptidase activity Source: InterPro
  • serine-type endopeptidase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • collagen catabolic process Source: Reactome
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.34. 2681.
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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7175. MMP8.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30888.

Chemistry

DrugBankiDB00786. Marimastat.

Polymorphism and mutation databases

BioMutaiMMP8.
DMDMi116862.

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

BgeeiP22894.
CleanExiHS_MMP8.
ExpressionAtlasiP22894. baseline and differential.
GenevisibleiP22894. HS.

Organism-specific databases

HPAiHPA021221.
HPA022935.

Interactioni

Protein-protein interaction databases

BioGridi110460. 1 interaction.
STRINGi9606.ENSP00000236826.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP22894.
KOiK01402.
OMAiEETWTKT.
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

        10         20         30         40         50
MFSLKTLPFL LLLHVQISKA FPVSSKEKNT KTVQDYLEKF YQLPSNQYQS
60 70 80 90 100
TRKNGTNVIV EKLKEMQRFF GLNVTGKPNE ETLDMMKKPR CGVPDSGGFM
110 120 130 140 150
LTPGNPKWER TNLTYRIRNY TPQLSEAEVE RAIKDAFELW SVASPLIFTR
160 170 180 190 200
ISQGEADINI AFYQRDHGDN SPFDGPNGIL AHAFQPGQGI GGDAHFDAEE
210 220 230 240 250
TWTNTSANYN LFLVAAHEFG HSLGLAHSSD PGALMYPNYA FRETSNYSLP
260 270 280 290 300
QDDIDGIQAI YGLSSNPIQP TGPSTPKPCD PSLTFDAITT LRGEILFFKD
310 320 330 340 350
RYFWRRHPQL QRVEMNFISL FWPSLPTGIQ AAYEDFDRDL IFLFKGNQYW
360 370 380 390 400
ALSGYDILQG YPKDISNYGF PSSVQAIDAA VFYRSKTYFF VNDQFWRYDN
410 420 430 440 450
QRQFMEPGYP KSISGAFPGI ESKVDAVFQQ EHFFHVFSGP RYYAFDLIAQ
460
RVTRVARGNK WLNCRYG
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:
EMBLi
GenBanki
DDBJi
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_001291370.1. NM_001304441.1.
NP_001291371.1. NM_001304442.1.
NP_002415.1. NM_002424.2.
UniGeneiHs.161839.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001291370.1. NM_001304441.1.
NP_001291371.1. NM_001304442.1.
NP_002415.1. NM_002424.2.
UniGeneiHs.161839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110460. 1 interaction.
STRINGi9606.ENSP00000236826.

Chemistry

BindingDBiP22894.
ChEMBLiCHEMBL4588.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1632.

Protein family/group databases

MEROPSiM10.002.

PTM databases

PhosphoSiteiP22894.

Polymorphism and mutation databases

BioMutaiMMP8.
DMDMi116862.

Proteomic databases

PaxDbiP22894.
PeptideAtlasiP22894.
PRIDEiP22894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4317.
GeneCardsiGC11M102617.
HGNCiHGNC:7175. MMP8.
HPAiHPA021221.
HPA022935.
MIMi120355. gene.
neXtProtiNX_P22894.
PharmGKBiPA30888.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258253.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP22894.
KOiK01402.
OMAiEETWTKT.
OrthoDBiEOG7XPZ57.
PhylomeDBiP22894.
TreeFamiTF315428.

Enzyme and pathway databases

BRENDAi3.4.24.34. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Miscellaneous databases

EvolutionaryTraceiP22894.
GeneWikiiMMP8.
GenomeRNAii4317.
NextBioi16985.
PMAP-CutDBP22894.
PROiP22894.
SOURCEiSearch...

Gene expression databases

BgeeiP22894.
CleanExiHS_MMP8.
ExpressionAtlasiP22894. baseline and differential.
GenevisibleiP22894. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.