3I77

35/99/170-loops of FXa in SGT

3I77 の概要

• エントリーDOI: 10.2210/pdb3i77/pdb
• 関連するPDBエントリー: 1OS8 2FMJ 3BEU 3I78
• 分子名称: Trypsin, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: beta sheets, serine protease, hydrolase, disulfide bond, protease, zymogen
• 由来する生物種: Streptomyces griseus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24396.19

構造登録者

Page, M.J.,Di Cera, E. (登録日: 2009-07-08, 公開日: 2010-06-02, 最終更新日: 2024-11-20)

主引用文献

Page, M.J.,Di Cera, E.
Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin Fold.
J.Mol.Biol., 399:306-319, 2010

PubMed Abstract: Converting one enzyme into another is challenging due to the uneven distribution of important amino acids for function in both protein sequence and structure. We report a strategy for protein engineering allowing an organized mixing and matching of genetic material that leverages lower throughput with increased quality of screens. Our approach successfully tested the contribution of each surface-exposed loop in the trypsin fold alone and the cooperativity of their combinations towards building the substrate selectivity and Na(+)-dependent allosteric activation of the protease domain of human coagulation factor Xa into a bacterial trypsin. As the created proteases lack additional protein domains and protein co-factor activation mechanism requisite for the complexity of blood coagulation, they are stepping-stones towards further understanding and engineering of artificial clotting factors.

PubMed: 20399789
DOI: 10.1016/j.jmb.2010.04.024

実験手法

X-RAY DIFFRACTION (2.1 Å)