2W9O

Solution structure of jerdostatin from Trimeresurus jerdonii

2W9O の概要

• エントリーDOI: 10.2210/pdb2w9o/pdb
• 関連するPDBエントリー: 2W9U 2W9V 2W9W
• NMR情報: BMRB: 16136
• 分子名称: SHORT DISINTEGRIN JERDOSTATIN (1 entity in total)
• 機能のキーワード: venom, toxin, cell adhesion, blood coagulation
• 由来する生物種: TRIMERESURUS JERDONII (JERDON'S PIT-VIPER)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4911.60

構造登録者

Carbajo, R.J.,Sanz, L.,Mosulen, S.,Calvete, J.J.,Pineda-Lucena, A. (登録日: 2009-01-27, 公開日: 2010-03-31, 最終更新日: 2024-11-20)

主引用文献

Carbajo, R.J.,Sanz, L.,Mosulen, S.,Perez, A.,Marcinkiewicz, C.,Pineda-Lucena, A.,Calvete, J.J.
NMR Structure and Dynamics of Recombinant Wild-Type and Mutated Jerdostatin, a Selective Inhibitor of Integrin Alpha1 Beta1
Proteins, 79:2530-, 2011

PubMed Abstract: NMR analysis of four recombinant jerdostatin molecules was assessed to define the structural basis of two naturally occurring gain-of-function events: C-terminal dipeptide processing and mutation of the active residue K21 to arginine. Removal of the highly mobile and a bulky C-terminal dipeptide produced pronounced chemical shift changes in the sequentially unconnected but spatially nearby α(1)β(1) inhibitory loop. Analysis of chemical shift divergence and (15)N backbone relaxation dynamics indicated differences in motions in the picosecond to nanosecond time scale, and the higher T(2) rate of S25, S26, and H27 of rJerK21 point to a slowdown in the microsecond to millisecond motions of these residues when compared with rJerR21. The evidence presented in this article converges on the hypothesis that dynamic differences between the α(1)β(1) recognition loops of rJerR21 and rJerK21 may influence the thermodynamics of their receptor recognition and binding. A decrease in the μs-ms time scale may impair the binding affinity by reducing the rate of possible conformations that the rJerK21 can adopt in this time scale.

PubMed: 21656569
DOI: 10.1002/PROT.23076

実験手法

SOLUTION NMR