2xu7

Structural basis for RbAp48 binding to FOG-1Structural basis for RbAp48 binding to FOG-1

Structural highlights 2xu7 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RBBP4_HUMAN Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. Publication Abstract from PubMed 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-Angstrom 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 beta-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 Metastasis Associated-1 (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 structure provides insight into the molecular determinants of FOG-1 dependent association with the NuRD complex and into the links between transcriptional regulation and nucleosome remodelling. Insights into the association of the nucleosome remodelling and deacetylase (NURD) complex with friend of gata-1 (FOG-1) from the crystal structure of a retinoblastoma associated protein-48 (RBAP48) fog-1 complex.,Lejon S, Thong SY, Murthy A, Alqarni S, Murzina NV, Blobel GA, Laue ED, Mackay JP J Biol Chem. 2010 Nov 2. PMID:21047798 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinoblastoma-binding protein 3D structures

spinqualitylabelsall models 2xu7, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image