2KOX

NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin

2KOX の概要

• エントリーDOI: 10.2210/pdb2kox/pdb
• 関連するPDBエントリー: 1d3z 1ubq 2k39 2nr2
• 分子名称: Ubiquitin (1 entity in total)
• 機能のキーワード: ubiquitin, residual dipolar coupling, simulated annealing, isopeptide bond, nucleus, phosphoprotein, signaling 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: 8576.83

構造登録者

Fenwick, R.B.,Richter, B.,Lee, D.,Walter, K.F.A.,Milovanovic, D.,Becker, S.,Lakomek, N.A.,Griesinger, C.,Salvatella, X. (登録日: 2009-10-02, 公開日: 2011-06-08, 最終更新日: 2024-05-01)

主引用文献

Fenwick, R.B.,Esteban-Martin, S.,Richter, B.,Lee, D.,Walter, K.F.A.,Milovanovic, D.,Becker, S.,Lakomek, N.A.,Griesinger, C.,Salvatella, X.
Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition
J.Am.Chem.Soc., 2011

PubMed Abstract: Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four β-strands separated by up to 15 Å in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network.

PubMed: 21634390
DOI: 10.1021/ja200461n

実験手法

SOLUTION NMR