1V6D

The crystal structure of the trypsin complex with synthetic heterochiral peptide

1V6D の概要

• エントリーDOI: 10.2210/pdb1v6d/pdb
• 関連するPDBエントリー: 1UHB
• 分子名称: Trypsin, PD(AIB)L(AIB)LA, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: trypsin complex, synthetic peptide, hydrolase
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24423.63

構造登録者

Shamaladevi, N.,Pattabhi, V. (登録日: 2003-11-28, 公開日: 2004-12-07, 最終更新日: 2023-11-15)

主引用文献

Shamaladevi, N.,Pattabhi, V.
Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex.
J.Biomol.Struct.Dyn., 22:635-642, 2005

PubMed Abstract: Designed synthetic heterochiral peptides, when added to porcine trypsin, resulted in reduction of enzyme activity. The crystal structure of a complex formed between porcine trypsin and a heterochiral hepta peptide Boc-Pro-DAsp-Aib-Leu-Aib-Leu-Ala-NHMe has been determined at 1.9 A resolution. The hepta peptide does not bind at the active site, but is located in the interstitial region, and interacts with the calcium-binding loop (residues 60-80). The bound peptide interacts with the active site residue Ser195 through an acetate ion, and with Lys 60 mediated by water molecules. The structure, when compared with the other trypsin-peptide complexes, suggests that the flexibility of surface loops, concerted movement of the loops towards the active site, and the interaction of the bound peptide with Lys 60, may be responsible for the reduction in enzyme activity. This study provides a structural evidence for the earlier biochemical observation regarding the role of surface loops in the catalysis of the enzyme.

PubMed: 15842169
DOI: 10.1080/07391102.2005.10507031

実験手法

X-RAY DIFFRACTION (1.9 Å)