5E11
Second PDZ domain of Ligand of Numb protein X 2 by Laue crystallography (no electric field)
5E11 の概要
| エントリーDOI | 10.2210/pdb5e11/pdb |
| 関連するPDBエントリー | 2VWR 5E1Y 5E21 5E22 |
| 分子名称 | Ligand of Numb protein X 2 (2 entities in total) |
| 機能のキーワード | unperturbed, off state., protein binding |
| 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 | 10310.74 |
| 構造登録者 | Hekstra, D.R.,White, K.I.,Socolich, M.A.,Henning, R.W.,Srajer, V.,Ranganathan, R. (登録日: 2015-09-29, 公開日: 2016-12-07, 最終更新日: 2026-03-04) |
| 主引用文献 | Hekstra, D.R.,White, K.I.,Socolich, M.A.,Henning, R.W.,Srajer, V.,Ranganathan, R. Electric-field-stimulated protein mechanics. Nature, 540:400-405, 2016 Cited by PubMed Abstract: The internal mechanics of proteins-the coordinated motions of amino acids and the pattern of forces constraining these motions-connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function. PubMed: 27926732DOI: 10.1038/nature20571 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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