2M85

PHD Domain from Human SHPRH

2M85 の概要

• エントリーDOI: 10.2210/pdb2m85/pdb
• 関連するPDBエントリー: 1WEP 1X4I 1XWH 2FUI 2JMI 2K16 2K1J 2KKG 2RSD 2VPD
• NMR情報: BMRB: 19229
• 分子名称: E3 ubiquitin-protein ligase SHPRH, ZINC ION (2 entities in total)
• 機能のキーワード: shprh, snf2, histone linker, phd finger, ring finger, helicase, hydrolase, ligase
• 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: 8720.73

構造登録者

Machado, L.E.S.F.,Pustovalova, Y.,Pozhidaeva, A.,Almeida, F.C.L.,Bezsonova, I.,Korzhnev, D.M. (登録日: 2013-05-07, 公開日: 2013-08-14, 最終更新日: 2024-05-01)

主引用文献

Machado, L.E.,Pustovalova, Y.,Kile, A.C.,Pozhidaeva, A.,Cimprich, K.A.,Almeida, F.C.,Bezsonova, I.,Korzhnev, D.M.
PHD domain from human SHPRH.
J.Biomol.Nmr, 56:393-399, 2013

PubMed Abstract: SHPRH (NF2, istone linker, HD, ING, elicase) is a SWI2/SNF2-family ATP-dependent chromatin remodeling factor, and one of E3 ubiquitin ligases responsible for Ubc13-Mms2-dependent K63 poly-ubiquitination of PCNA (roliferating ell uclear ntigen) that promotes error-free DNA damage tolerance in eukaryotes. In contrast to its functional homologues, Rad5 and human HLTF (elicase ike ranscription actor), SHPRH contains a PHD (lant omeoomain) finger embedded in the ‘minor’ insert region of the core helicase-like domain. PHD fingers are often found in proteins involved in chromatin remodeling and transcription regulation, and are generally considered as ‘readers’ of methylation state of histone tails, primarily the lysine 4 (K4) residue of histone H3 (H3K4). Here we report the solution NMR structure of the SHPRH PHD domain and investigate whether this domain is capable of recognizing H3K4 modifications. The domain adopts a canonical PHD-finger fold with a central two-stranded anti-parallel β-sheet flanked on both sides by the two interleaved zinc-binding sites. Despite the presence of a subset of aromatic residues characteristic for PHD-fingers that preferentially bind methylated H3K4, NMR titration experiments reveal that SHPRH PHD does not specifically interact with the H3-derived peptides irrespective of K4 methylation. This result suggests that the SHPRH PHD domain might have evolved a different function other than recognizing histone modifications.

PubMed: 23907177
DOI: 10.1007/s10858-013-9758-2

実験手法

SOLUTION NMR