2XU7

Structural basis for RbAp48 binding to FOG-1

2XU7 の概要

• エントリーDOI: 10.2210/pdb2xu7/pdb
• 分子名称: HISTONE-BINDING PROTEIN RBBP4, ZINC FINGER PROTEIN ZFPM1, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: transcription, chromatin remodelling, histone chaperone, corepressor, gata1-mediated repression, nurd complex
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: Q09028; Nucleus (By similarity): Q8IX07
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 99563.93

構造登録者

Lejon, S.,Thong, S.Y.,Murthy, A.,Blobel, G.A.,Mackay, J.P.,Murzina, N.V.,Laue, E.D. (登録日: 2010-10-15, 公開日: 2010-11-03, 最終更新日: 2023-12-20)

主引用文献

Lejon, S.,Thong, S.Y.,Murthy, A.,Alqarni, S.,Murzina, N.V.,Blobel, G.A.,Laue, E.D.,Mackay, J.P.
Insights Into Association of the Nurd Complex with Fog-1 from the Crystal Structure of an Rbap48-Fog- 1 Complex.
J.Biol.Chem., 286:1196-, 2011

PubMed Abstract: Chromatin-modifying complexes such as the NuRD complex are recruited to particular genomic sites by gene-specific nuclear factors. Overall, however, little is known about the molecular basis for these interactions. Here, we present the 1.9 Å resolution crystal structure of the NuRD subunit RbAp48 bound to the 15 N-terminal amino acids of the GATA-1 cofactor FOG-1. The FOG-1 peptide contacts a negatively charged binding pocket on top of the RbAp48 β-propeller that is distinct from the binding surface used by RpAp48 to contact histone H4. We further show that RbAp48 interacts with the NuRD subunit MTA-1 via a surface that is distinct from its FOG-binding pocket, providing a first glimpse into the way in which NuRD assembly facilitates interactions with cofactors. Our RbAp48·FOG-1 structure provides insight into the molecular determinants of FOG-1-dependent association with the NuRD complex and into the links between transcription regulation and nucleosome remodeling.

PubMed: 21047798
DOI: 10.1074/JBC.M110.195842

実験手法

X-RAY DIFFRACTION (1.9 Å)