2aiq: Difference between revisions

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[[Image:2aiq.gif|left|200px]]
{{Seed}}
[[Image:2aiq.png|left|200px]]


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{{STRUCTURE_2aiq|  PDB=2aiq  |  SCENE=  }}  
{{STRUCTURE_2aiq|  PDB=2aiq  |  SCENE=  }}  


'''Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix'''
===Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix===




==Overview==
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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-).
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{{ABSTRACT_PUBMED_16162508}}


==About this Structure==
==About this Structure==
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[[Category: Protein c activator]]
[[Category: Protein c activator]]
[[Category: Snake venom serine proteinase]]
[[Category: Snake venom serine proteinase]]
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