6SVC

Protein allostery of the WW domain at atomic resolution: apo structure

6SVC の概要

• エントリーDOI: 10.2210/pdb6svc/pdb
• 関連するPDBエントリー: 6SVE 6SVH
• NMR情報: BMRB: 34432
• 分子名称: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (1 entity in total)
• 機能のキーワード: structure from cyana 3.98.12, peptide binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4105.58

構造登録者

Strotz, D.,Orts, J.,Friedmann, M.,Guntert, P.,Vogeli, B.,Riek, R. (登録日: 2019-09-18, 公開日: 2020-09-30, 最終更新日: 2024-06-19)

主引用文献

Strotz, D.,Orts, J.,Kadavath, H.,Friedmann, M.,Ghosh, D.,Olsson, S.,Chi, C.N.,Pokharna, A.,Guntert, P.,Vogeli, B.,Riek, R.
Protein Allostery at Atomic Resolution.
Angew.Chem.Int.Ed.Engl., 59:22132-22139, 2020

PubMed Abstract: Protein allostery is a phenomenon involving the long range coupling between two distal sites in a protein. In order to elucidate allostery at atomic resoluion on the ligand-binding WW domain of the enzyme Pin1, multistate structures were calculated from exact nuclear Overhauser effect (eNOE). In its free form, the protein undergoes a microsecond exchange between two states, one of which is predisposed to interact with its parent catalytic domain. In presence of the positive allosteric ligand, the equilibrium between the two states is shifted towards domain-domain interaction, suggesting a population shift model. In contrast, the allostery-suppressing ligand decouples the side-chain arrangement at the inter-domain interface thereby reducing the inter-domain interaction. As such, this mechanism is an example of dynamic allostery. The presented distinct modes of action highlight the power of the interplay between dynamics and function in the biological activity of proteins.

PubMed: 32797659
DOI: 10.1002/anie.202008734

実験手法

SOLUTION NMR