6BPH
Crystal structure of the chromodomain of RBBP1
Summary for 6BPH
Entry DOI | 10.2210/pdb6bph/pdb |
Descriptor | AT-rich interactive domain-containing protein 4A, UNKNOWN ATOM OR ION (3 entities in total) |
Functional Keywords | crystal structure of the chromodomain of rbbp1, structural genomics, structural genomics consortium, sgc, unknown function |
Biological source | Homo sapiens (Human) |
Cellular location | Nucleus : P29374 |
Total number of polymer chains | 1 |
Total formula weight | 8068.16 |
Authors | Liu, Y.,Tempel, W.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2017-11-23, release date: 2017-12-20, Last modification date: 2024-11-06) |
Primary citation | Lei, M.,Feng, Y.,Zhou, M.,Yang, Y.,Loppnau, P.,Li, Y.,Yang, Y.,Liu, Y. Crystal structure of chromo barrel domain of RBBP1. Biochem. Biophys. Res. Commun., 496:1344-1348, 2018 Cited by PubMed Abstract: RBBP1 is a retinoblastoma protein (pRb) binding protein acting as a repressor of gene transcription. RBBP1 is a multidomain protein including a chromo barrel domain, and its chromo barrel domain has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. However, the molecular basis of this DNA-mediated histone binding by the chromo barrel domain of RBBP1 is unclear. Here we attempted to co-crystallize the chromo barrel domain of RBBP1 with either a histone H4K20me3 peptide alone or with both a histone H4K20me3 peptide and DNA, but only solved the peptide/DNA unbound crystal structure. Our structural analysis indicates that RBBP1 could interact with histone H4K20me3 similar to other histone binding chromo barrel domains, and the surface charge representation analysis of the chromo barrel domain of RBBP1 suggests that the chromo barrel domain of RBBP1 does not have a typical DNA binding surface, indicating that it might not bind to DNA. Consistently, our ITC assays also showed that DNA does not significantly enhance the histone binding ability of the chromo barrel domain of RBBP1. PubMed: 29408527DOI: 10.1016/j.bbrc.2018.02.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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