2AIP

Crystal structure of native protein C activator from the venom of copperhead snake Agkistrodon contortrix contortrix

2AIP の概要

• エントリーDOI: 10.2210/pdb2aip/pdb
• 分子名称: Protein C activator, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: protein c activator, snake venom, trypsin-like enzyme, hydrolase
• 由来する生物種: Agkistrodon contortrix contortrix (southern copperhead)
• 細胞内の位置: Secreted: P09872
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26235.83

構造登録者

Murakami, M.T.,Arni, R.K. (登録日: 2005-07-30, 公開日: 2005-09-06, 最終更新日: 2024-11-20)

主引用文献

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

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: 16162508
DOI: 10.1074/jbc.M508502200

実験手法

X-RAY DIFFRACTION (1.65 Å)