3BEF

Crystal structure of thrombin bound to the extracellular fragment of PAR1

3BEF の概要

• エントリーDOI: 10.2210/pdb3bef/pdb
• 関連するPDBエントリー: 1SHH 2GP9 3BEI
• 分子名称: Prothrombin, Proteinase-activated receptor 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: serine protease, acute phase, blood coagulation, cleavage on pair of basic residues, disease mutation, gamma-carboxyglutamic acid, glycoprotein, hydrolase, kringle, secreted, zymogen, g-protein coupled receptor, membrane, phosphoprotein, receptor, transducer, transmembrane
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 73193.24

構造登録者

Gandhi, P.S.,Bah, A.,Chen, Z.,Mathews, F.S.,Di Cera, E. (登録日: 2007-11-17, 公開日: 2008-01-01, 最終更新日: 2024-10-30)

主引用文献

Gandhi, P.S.,Chen, Z.,Mathews, F.S.,Di Cera, E.
Structural identification of the pathway of long-range communication in an allosteric enzyme.
Proc.Natl.Acad.Sci.Usa, 105:1832-1837, 2008

PubMed Abstract: Allostery is a common mechanism of regulation of enzyme activity and specificity, and its signatures are readily identified from functional studies. For many allosteric systems, structural evidence exists of long-range communication among protein domains, but rarely has this communication been traced to a detailed pathway. The thrombin mutant D102N is stabilized in a self-inhibited conformation where access to the active site is occluded by a collapse of the entire 215-219 beta-strand. Binding of a fragment of the protease activated receptor PAR1 to exosite I, 30-A away from the active site region, causes a large conformational change that corrects the position of the 215-219 beta-strand and restores access to the active site. The crystal structure of the thrombin-PAR1 complex, solved at 2.2-A resolution, reveals the details of this long-range allosteric communication in terms of a network of polar interactions.

PubMed: 18250335
DOI: 10.1073/pnas.0710894105

実験手法

X-RAY DIFFRACTION (2.2 Å)