1TWX

Crystal structure of the thrombin mutant D221A/D222K

1TWX の概要

• エントリーDOI: 10.2210/pdb1twx/pdb
• 分子名称: Prothrombin, Hirudin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: thrombin, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 34566.56

構造登録者

Pineda, A.O.,Zhang, E.,Guinto, E.R.,Savvides, S.N.,Tulinsky, A.,Di Cera, E. (登録日: 2004-07-01, 公開日: 2005-04-19, 最終更新日: 2024-11-06)

主引用文献

Pineda, A.O.,Zhang, E.,Guinto, E.R.,Savvides, S.N.,Tulinsky, A.,Di Cera, E.
Crystal structure of the thrombin mutant D221A/D222K: the Asp222:Arg187 ion-pair stabilizes the fast form
Biophys.Chem., 112:253-256, 2004

PubMed Abstract: The thrombin mutant D221A/D222K (ARK) does not bind Na+ and has interesting functional properties intermediate between those of the slow and fast forms of wild type. We solved the X-ray crystal structure of ARK bound at exosite I with a fragment of hirudin at 2.4-A resolution. The structure shows a slight collapse of the 186 and 220 loops into the Na+ binding site due to disruption of the Asp222:Arg187 ion-pair. The backbone O atoms of Arg221a and Lys224 are shifted into conformations that eliminate optimal interaction with Na+. A paucity of solvent molecules in the Na+ binding site is also noted, by analogy to what is seen in the structure of the slow form. These findings reinforce the crucial role of the Asp222:Arg187 ion-pair in stabilizing the fast form of thrombin.

PubMed: 15572256
DOI: 10.1016/j.bpc.2004.07.027

実験手法

X-RAY DIFFRACTION (2.4 Å)