UniProt release 11.3
Published July 10, 2007
Knottins or how to knit in the protein world
Knottins (also called inhibitor cystine knots or ICKs) are small disulfide-rich proteins characterized by a special "disulfide through disulfide knot". This knot is obtained when one disulfide bridge crosses the macrocycle formed by two other disulfides and the interconnecting backbone (disulfide 3-6 goes through disulfides 1-4 and 2-5).
The knottin structure is found in many unrelated families, such as plant protease inhibitors, cyclotides, toxins from cone snails, spiders, insects, horseshoe crabs and scorpions, gurmarin-like peptides, agouti-related proteins, and antimicrobial peptides.
In collaboration with Laurent Chiche (CNRS, Montpellier), about 450 UniProtKB/Swiss-Prot entries have been updated with knottin structural information. They can be retrieved with the newly introduced keyword Knottin.
Cross-references to PharmGKB
Cross-references have been added to the PharmGKB database. PharmGKB curates information that establishes knowledge about the relationships among drugs, diseases and genes, including their variations and gene products. It is a repository for genetic, genomic, molecular and cellular phenotype data and clinical information about people who have participated in pharmacogenomics research studies. The data includes, but is not limited to, clinical and basic pharmacokinetic and pharmacogenomic research in the cardiovascular, pulmonary, cancer, pathways, metabolic and transporter domains.
The PharmGKB database is available at http://www.pharmgkb.org/.
The format of the explicit links in the flat file is:
|Resource identifier||PharmGKB accession ID.|
Q96S55: DR PharmGKB; PA134982239; -.
Changes concerning keywords