2FO8

Solution structure of the Trypanosoma cruzi cysteine protease inhibitor chagasin

2FO8 の概要

• エントリーDOI: 10.2210/pdb2fo8/pdb
• 関連するPDBエントリー: 2C34
• NMR情報: BMRB: 6876
• 分子名称: Chagasin (1 entity in total)
• 機能のキーワード: chagasin; ig-like domain; cysteine protease inhibitor; trypanosoma cruzi, hydrolase inhibitor
• 由来する生物種: Trypanosoma cruzi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12067.41

構造登録者

Salmon, D.,do Aido-Machado, R.,de Lima, A.A.P.,Scharfstein, J.,Oschkinat, H.,Pires, J.R. (登録日: 2006-01-13, 公開日: 2006-04-04, 最終更新日: 2024-05-08)

主引用文献

Salmon, D.,do Aido-Machado, R.,Diehl, A.,Leidert, M.,Schmetzer, O.,de Lima, A.A.P.,Scharfstein, J.,Oschkinat, H.,Pires, J.R.
Solution Structure and Backbone Dynamics of the Trypanosoma cruzi Cysteine Protease Inhibitor Chagasin
J.Mol.Biol., 357:1511-1521, 2006

PubMed Abstract: A Trypanosoma cruzi cysteine protease inhibitor, termed chagasin, is the first characterized member of a new family of tight-binding cysteine protease inhibitors identified in several lower eukaryotes and prokaryotes but not present in mammals. In the protozoan parasite T.cruzi, chagasin plays a role in parasite differentiation and in mammalian host cell invasion, due to its ability to modulate the endogenous activity of cruzipain, a lysosomal-like cysteine protease. In the present work, we determined the solution structure of chagasin and studied its backbone dynamics by NMR techniques. Structured as a single immunoglobulin-like domain in solution, chagasin exerts its inhibitory activity on cruzipain through conserved residues placed in three loops in the same side of the structure. One of these three loops, L4, predicted to be of variable length among chagasin homologues, is flexible in solution as determined by measurements of (15)N relaxation. The biological implications of structural homology between chagasin and other members of the immunoglobulin super-family are discussed.

PubMed: 16490204
DOI: 10.1016/j.jmb.2006.01.064

実験手法

SOLUTION NMR