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2XU7

Structural basis for RbAp48 binding to FOG-1

Summary for 2XU7
Entry DOI10.2210/pdb2xu7/pdb
DescriptorHISTONE-BINDING PROTEIN RBBP4, ZINC FINGER PROTEIN ZFPM1, TETRAETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywordstranscription, chromatin remodelling, histone chaperone, corepressor, gata1-mediated repression, nurd complex
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationNucleus: Q09028
Nucleus (By similarity): Q8IX07
Total number of polymer chains4
Total formula weight99563.93
Authors
Lejon, S.,Thong, S.Y.,Murthy, A.,Blobel, G.A.,Mackay, J.P.,Murzina, N.V.,Laue, E.D. (deposition date: 2010-10-15, release date: 2010-11-03, Last modification date: 2023-12-20)
Primary citationLejon, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2025-07-23公开中

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