1JBU

Coagulation Factor VII Zymogen (EGF2/Protease) in Complex with Inhibitory Exosite Peptide A-183

1JBU の概要

• エントリーDOI: 10.2210/pdb1jbu/pdb
• 関連するPDBエントリー: 1CVW 1DAN 1DVA 1FAK 1QFK
• 分子名称: COAGULATION FACTOR VII, Peptide exosite inhibitor A-183, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: shifted registration, beta-strands, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P08709 P08709
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 37191.41

構造登録者

Eigenbrot, C.,Kirchhofer, D.,Dennis, M.S.,Santell, L.,Lazarus, R.A.,Stamos, J.,Ultsch, M.H. (登録日: 2001-06-06, 公開日: 2001-07-11, 最終更新日: 2024-10-30)

主引用文献

Eigenbrot, C.,Kirchhofer, D.,Dennis, M.S.,Santell, L.,Lazarus, R.A.,Stamos, J.,Ultsch, M.H.
The factor VII zymogen structure reveals reregistration of beta strands during activation.
Structure, 9:627-636, 2001

PubMed Abstract: Coagulation factor VIIa (FVIIa) contains a Trypsin-like serine protease domain and initiates the cascade of proteolytic events leading to Thrombin activation and blood clot formation. Vascular injury allows formation of the complex between circulating FVIIa and its cell surface bound obligate cofactor, Tissue Factor (TF). Circulating FVIIa is nominally activated but retains zymogen-like character and requires TF in order to complete the zymogen-to-enzyme transition. The manner in which TF exerts this effect is unclear. The structure of TF/FVIIa is known. Knowledge of the zymogen structure is helpful for understanding the activation transition in this system.

PubMed: 11470437
DOI: 10.1016/S0969-2126(01)00624-4

実験手法

X-RAY DIFFRACTION (2 Å)