Structural highlights
Function
SLUA_DEIAC Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX (F9) and factor X (F10) in the presence of calcium with a 1 to 1 stoichiometry. Also inhibits platelet aggregation by binding to platelet glycoprotein Ibalpha (GP1BA) and functioning as a blocker of von Willebrand factor (VWF). Is devoid of hemorrhagic and lethal activities. Possesses antithrombotic and thrombolytic activities. Also hydrolyzes the Aalpha-chain of fibrinogen (FGA). Does not affect the Bbeta-chain (FGB) and the gamma chain (FGG).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Cheng X, Qian Y, Liu Q, Li BX, Zhang M, Liu J. Purification, characterization, and cDNA cloning of a new fibrinogenlytic venom protein, Agkisacutacin, from Agkistrodon acutus venom. Biochem Biophys Res Commun. 1999 Nov 19;265(2):530-5. PMID:10558903 doi:10.1006/bbrc.1999.1685
- ↑ Cheng X, Xu ZY, Liu QD, Li XM, Li XY, Liu J. Purification and Characterization of a Platelet Agglutinating Inhibiting Protein (Agkisacutacin) from Agkistrodon acutus Venom. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(6):653-656 PMID:12058182
- ↑ Li WF, Chen L, Li XM, Liu J. A C-type lectin-like protein from Agkistrodon acutus venom binds to both platelet glycoprotein Ib and coagulation factor IX/factor X. Biochem Biophys Res Commun. 2005 Jul 8;332(3):904-12. PMID:15925567 doi:10.1016/j.bbrc.2005.05.033
