2AIQ
Crystal structure of benzamidine-inhibited protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix
Summary for 2AIQ
| Entry DOI | 10.2210/pdb2aiq/pdb |
| Related | 2AIP |
| Descriptor | Protein C activator, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (8 entities in total) |
| Functional Keywords | protein c activator, snake venom serine proteinase, hydrolase |
| Biological source | Agkistrodon contortrix contortrix (southern copperhead) |
| Cellular location | Secreted: P09872 |
| Total number of polymer chains | 1 |
| Total formula weight | 26199.31 |
| Authors | Murakami, M.T.,Arni, R.K. (deposition date: 2005-07-30, release date: 2005-09-06, Last modification date: 2024-11-06) |
| Primary citation | Murakami, M.T.,Arni, R.K. 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. J.Biol.Chem., 280:39309-39315, 2005 Cited by PubMed Abstract: 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-). PubMed: 16162508DOI: 10.1074/jbc.M508502200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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