Structural highlights
Function
[XA2_DEIAC] Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX and factor X 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 vWF. Is devoid of hemorrhagic and lethal activities. Possess antithrombotic and thrombolytic activities. Also hydrolyzes the Aalpha-chain of fibrinogen. Does not affect the Bbeta-chain and the gamma chain (By similarity).[1] [XB2_DEIAC] Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX and factor X 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 vWF. Is devoid of hemorrhagic and lethal activities. Possess antithrombotic and thrombolytic activities. Also hydrolyzes the Aalpha-chain of fibrinogen. Does not affect the Bbeta-chain and the gamma chain (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Tani A, Ogawa T, Nose T, Nikandrov NN, Deshimaru M, Chijiwa T, Chang CC, Fukumaki Y, Ohno M. Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom. Toxicon. 2002 Jun;40(6):803-13. PMID:12175618
