4BHP

A structural model of CAP mutant (T127L and S128I) in cGMP-bound state

4BHP の概要

• エントリーDOI: 10.2210/pdb4bhp/pdb
• 関連するPDBエントリー: 4BH9
• NMR情報: BMRB: 19145
• 分子名称: CAMP RECEPTOR PROTEIN (1 entity in total)
• 機能のキーワード: transcription
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23579.38

構造登録者

Tzeng, S.R.,Kalodimos, C.G. (登録日: 2013-04-04, 公開日: 2013-05-08, 最終更新日: 2024-06-19)

主引用文献

Tzeng, S.R.,Kalodimos, C.G.
Allosteric Inhibition Through Suppression of Transient Conformational States.
Nat.Chem.Biol., 9:462-, 2013

PubMed Abstract: The ability to inhibit binding or enzymatic activity is key to preventing aberrant behaviors of proteins. Allosteric inhibition is desirable as it offers several advantages over competitive inhibition, but the mechanisms of action remain poorly understood in most cases. Here we show that allosteric inhibition can be effected by destabilizing a low-populated conformational state that serves as an on-pathway intermediate for ligand binding, without altering the protein's ground-state structure. As standard structural approaches are typically concerned with changes in the ground-state structure of proteins, the presence of such a mechanism can go easily undetected. Our data strongly argue for the routine use of NMR tools suited to detect and characterize transiently formed conformational states in allosteric systems. Structure information on such important intermediates can ultimately result in more efficient design of allosteric inhibitors.

PubMed: 23644478
DOI: 10.1038/NCHEMBIO.1250

実験手法

SOLUTION NMR