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2HWL

Crystal structure of thrombin in complex with fibrinogen gamma' peptide

2HWL の概要
エントリーDOI10.2210/pdb2hwl/pdb
分子名称Prothrombin, Fibrinogen gamma' peptide, SODIUM ION, ... (6 entities in total)
機能のキーワードthrombin, fibrinogen, gamma' peptide, serine protease structure, allostery, hydrolase
由来する生物種Homo sapiens (human)
詳細
タンパク質・核酸の鎖数5
化学式量合計69652.03
構造登録者
Pineda, A.O.,Chen, Z.W.,Marino, F.,Mathews, F.S.,Mosesson, M.W.,Di Cera, E. (登録日: 2006-08-01, 公開日: 2006-09-19, 最終更新日: 2024-11-06)
主引用文献Pineda, A.O.,Chen, Z.W.,Marino, F.,Mathews, F.S.,Mosesson, M.W.,Di Cera, E.
Crystal structure of thrombin in complex with fibrinogen gamma' peptide.
Biophys.Chem., 125:556-559, 2007
Cited by
PubMed Abstract: Elevated levels of heterodimeric gamma(A)/gamma' fibrinogen 2 have been associated with an increased incidence of coronary artery disease, whereas a lowered content of gamma' chains is associated with an increased risk of venous thrombosis. Both situations may be related to the unique features of thrombin binding to variant gamma' chains. The gamma' peptide is an anionic fragment that binds thrombin with high affinity without interfering directly with substrate binding. Here we report the crystal structure of thrombin bound to the gamma' peptide, solved at 2.4 A resolution. The complex reveals extensive interactions between thrombin and the gamma' peptide mediated by electrostatic contacts with residues of exosite II and hydrophobic interactions with a pocket in close proximity to the Na(+) binding site. In its binding mode, the gamma' peptide completely overlaps with heparin bound to exosite II. These findings are consistent with functional data and broaden our understanding of how thrombin interacts with fibrinogen at the molecular level.
PubMed: 16962697
DOI: 10.1016/j.bpc.2006.08.005
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 2hwl
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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