2aip
Crystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix
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OverviewOverview
Protein C activation initiated by the thrombin-thrombomodulin complex, forms the major physiological anticoagulant pathway. Agkistrodon, contortrix contortrix protein C activator, a glycosylated single-chain, serine proteinase, activates protein C without relying on thrombomodulin., The crystal structures of native and inhibited Agkistrodon contortrix, contortrix protein C activator determined at 1.65 and 1.54 A resolutions, respectively, indicate the pivotal roles played by the positively charged, belt and the strategic positioning of the three carbohydrate moieties, surrounding the catalytic site in protein C recognition, binding, and, activation. Structural changes in the benzamidine-inhibited enzyme suggest, a probable function in allosteric regulation for the anion-binding site, located in the C-terminal extension, which is fully conserved in snake, venom serine proteinases, that preferentially binds Cl(1-) instead of, SO(4)(2-).
About this StructureAbout this Structure
2AIP is a Single protein structure of sequence from Agkistrodon contortrix contortrix with NAG, NDG, SO4, ACT and GOL as ligands. Active as Venombin A, with EC number 3.4.21.74 Full crystallographic information is available from OCA.
ReferenceReference
Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator., Murakami MT, Arni RK, J Biol Chem. 2005 Nov 25;280(47):39309-15. Epub 2005 Sep 14. PMID:16162508
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