| Disintegrin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of disintegrin heterodimer from Echis carinatus | |||||||||
| Identifiers | |||||||||
| Symbol | Disintegrin | ||||||||
| Pfam | PF00200 | ||||||||
| InterPro | IPR001762 | ||||||||
| PROSITE | PDOC00351 | ||||||||
| SCOP2 | 1kst / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 227 | ||||||||
| OPM protein | 2ao7 | ||||||||
| Membranome | 538 | ||||||||
| |||||||||
Disintegrins are a family of small proteins (45–84 amino acids in length) from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion.[1][2][3]
- ^ Oliveira, Ana L.; Viegas, Matilde F.; da Silva, Saulo L.; Soares, Andreimar M.; Ramos, Maria J.; Fernandes, Pedro A. (July 2022). "The chemistry of snake venom and its medicinal potential". Nature Reviews Chemistry. 6 (7): 451–469. doi:10.1038/s41570-022-00393-7. ISSN 2397-3358. PMC 9185726.
- ^ McLane MA, Sanchez EE, Wong A, Paquette-Straub C, Perez JC (2004). "Disintegrins". Curr Drug Targets Cardiovasc Haematol Disord. 4 (4): 327–55. doi:10.2174/1568006043335880. PMID 15578957.
- ^ Lu X, Lu D, Scully MF, Kakkar VV (2005). "Snake venom metalloproteinase containing a disintegrin-like domain, its structure-activity relationships at interacting with integrins". Curr Med Chem Cardiovasc Hematol Agents. 3 (3): 249–60. doi:10.2174/1568016054368205. PMID 15974889.