Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5JH5

Structural Basis for the Hierarchical Assembly of the Core of PRC1.1

Summary for 5JH5
Entry DOI10.2210/pdb5jh5/pdb
DescriptorLysine-specific demethylase 2B, S-phase kinase-associated protein 1, Polycomb group RING finger protein 1, ... (5 entities in total)
Functional Keywordsgene repression, complex, transcription regulation, transcription repressor, metal binding protein-transcription complex, metal binding protein/transcription
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus, nucleolus : Q8NHM5
Nucleus : Q9BSM1 Q5H9F3
Total number of polymer chains4
Total formula weight78554.55
Authors
Wong, S.J.,Taylor, A.B.,Hart, P.J.,Kim, C.A. (deposition date: 2016-04-20, release date: 2016-09-14, Last modification date: 2024-10-23)
Primary citationWong, S.J.,Gearhart, M.D.,Taylor, A.B.,Nanyes, D.R.,Ha, D.J.,Robinson, A.K.,Artigas, J.A.,Lee, O.J.,Demeler, B.,Hart, P.J.,Bardwell, V.J.,Kim, C.A.
KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1.
Structure, 24:1795-1801, 2016
Cited by
PubMed Abstract: KDM2B recruits H2A-ubiquitinating activity of a non-canonical Polycomb Repression Complex 1 (PRC1.1) to CpG islands, facilitating gene repression. We investigated the molecular basis of recruitment using in vitro assembly assays to identify minimal components, subcomplexes, and domains required for recruitment. A minimal four-component PRC1.1 complex can be assembled by combining two separately isolated subcomplexes: the DNA-binding KDM2B/SKP1 heterodimer and the heterodimer of BCORL1 and PCGF1, a core component of PRC1.1. The crystal structure of the KDM2B/SKP1/BCORL1/PCGF1 complex illustrates the crucial role played by the PCGF1/BCORL1 heterodimer. The BCORL1 PUFD domain positions residues preceding the RAWUL domain of PCGF1 to create an extended interface for interaction with KDM2B, which is unique to the PCGF1-containing PRC1.1 complex. The structure also suggests how KDM2B might simultaneously function in PRC1.1 and an SCF ubiquitin ligase complex and the possible molecular consequences of BCOR PUFD internal tandem duplications found in pediatric kidney and brain tumors.
PubMed: 27568929
DOI: 10.1016/j.str.2016.07.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon