1ATE

HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE

1ATE の概要

• エントリーDOI: 10.2210/pdb1ate/pdb
• 分子名称: ASCARIS TRYPSIN INHIBITOR (1 entity in total)
• 機能のキーワード: proteinase inhibitor(trypsin)
• 由来する生物種: Ascaris suum (pig roundworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6807.85

構造登録者

Clore, G.M.,Grasberger, B.L.,Gronenborn, A.M. (登録日: 1994-05-20, 公開日: 1994-08-31, 最終更新日: 2024-10-16)

主引用文献

Grasberger, B.L.,Clore, G.M.,Gronenborn, A.M.
High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site.
Structure, 2:669-678, 1994

PubMed Abstract: The Ascaris trypsin inhibitor (ATI) is a member of a new family of serine protease inhibitors isolated from the helminthic worm Ascaris lumbricoides var suum. This family comprises five chymotrypsin/elastase inhibitors and one trypsin inhibitor. Members are characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues.

PubMed: 7922043
DOI: 10.1016/S0969-2126(00)00067-8

実験手法

SOLUTION NMR