5C0M

Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide

5C0M の概要

• エントリーDOI: 10.2210/pdb5c0m/pdb
• 分子名称: SAGA-associated factor 29 homolog, Carba-containing peptide, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: sgf29, tandem tudor domain, carba containing peptide, structural genomics, structural genomics consortium, sgc, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q96ES7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 43068.95

構造登録者

Dong, A.,Xu, C.,Tempel, W.,Cerovina, T.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2015-06-12, 公開日: 2015-07-01, 最終更新日: 2023-11-15)

主引用文献

Kamps, J.J.,Huang, J.,Poater, J.,Xu, C.,Pieters, B.J.,Dong, A.,Min, J.,Sherman, W.,Beuming, T.,Matthias Bickelhaupt, F.,Li, H.,Mecinovic, J.
Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.
Nat Commun, 6:8911-8911, 2015

PubMed Abstract: A large number of structurally diverse epigenetic reader proteins specifically recognize methylated lysine residues on histone proteins. Here we describe comparative thermodynamic, structural and computational studies on recognition of the positively charged natural trimethyllysine and its neutral analogues by reader proteins. This work provides experimental and theoretical evidence that reader proteins predominantly recognize trimethyllysine via a combination of favourable cation-π interactions and the release of the high-energy water molecules that occupy the aromatic cage of reader proteins on the association with the trimethyllysine side chain. These results have implications in rational drug design by specifically targeting the aromatic cage of readers of trimethyllysine.

PubMed: 26578293
DOI: 10.1038/ncomms9911

実験手法

X-RAY DIFFRACTION (1.6 Å)