2XU7
Structural basis for RbAp48 binding to FOG-1
Summary for 2XU7
Entry DOI | 10.2210/pdb2xu7/pdb |
Descriptor | HISTONE-BINDING PROTEIN RBBP4, ZINC FINGER PROTEIN ZFPM1, TETRAETHYLENE GLYCOL, ... (4 entities in total) |
Functional Keywords | transcription, chromatin remodelling, histone chaperone, corepressor, gata1-mediated repression, nurd complex |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Nucleus: Q09028 Nucleus (By similarity): Q8IX07 |
Total number of polymer chains | 4 |
Total formula weight | 99563.93 |
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 citation | 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 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: 21047798DOI: 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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