Title : Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibalpha. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibalpha as a binding site for von Willebrand factor and alpha-thrombin.

Pub. Date : 1996 Apr 16

PMID : 8664285






3 Functional Relationships(s)
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1 In ligand blot analysis, thrombin blotted the His-1-Glu-282 fragment, but not His-1-Leu-275. Histidine coagulation factor II, thrombin Homo sapiens
2 These findings indicate that the sulfated tyrosine/anionic GP Ibalpha residues Tyr-276-Glu-282 are important for the binding of thrombin and botrocetin-dependent binding of thrombin and the botrocetin-dependent binding of vWF, but that vWF also interacts with residues within His-1-Leu-275. Histidine coagulation factor II, thrombin Homo sapiens
3 These findings indicate that the sulfated tyrosine/anionic GP Ibalpha residues Tyr-276-Glu-282 are important for the binding of thrombin and botrocetin-dependent binding of thrombin and the botrocetin-dependent binding of vWF, but that vWF also interacts with residues within His-1-Leu-275. Histidine coagulation factor II, thrombin Homo sapiens