Structural highlights
Function
[VM2RH_CALRH] Metalloproteinase rhodostoxin: snake venom metalloproteinase that impairs hemostasis in the envenomed animal (By similarity). Disintegrin rhodostomin: inhibit platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein.
Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist.,Adler M, Lazarus RA, Dennis MS, Wagner G Science. 1991 Jul 26;253(5018):445-8. PMID:1862345[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Adler M, Lazarus RA, Dennis MS, Wagner G. Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist. Science. 1991 Jul 26;253(5018):445-8. PMID:1862345
