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4HPM

PCGF1 Ub fold (RAWUL)/BCORL1 PUFD Complex

Summary for 4HPM
Entry DOI10.2210/pdb4hpm/pdb
Related4HPL
DescriptorBCL-6 corepressor-like protein 1, Polycomb group RING finger protein 1, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordspolycomb, bcorl1, pcgf1, rawul, nspc1, e3-ligase, chromosomal protein, transcription regulation, chromatin regulator, transcription repressor, ligase, metal-binding, nucleus, repressor, transcription, ubl conjugation pathway, zinc-finger
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: Q5H9F3 Q9BSM1
Total number of polymer chains4
Total formula weight50575.80
Authors
Junco, S.E.,Wang, R.,Gaipa, J.,Taylor, A.B.,Gearhart, M.D.,Bardwell, V.J.,Hart, P.J.,Kim, C.A. (deposition date: 2012-10-24, release date: 2013-05-01, Last modification date: 2024-11-20)
Primary citationJunco, S.E.,Wang, R.,Gaipa, J.C.,Taylor, A.B.,Schirf, V.,Gearhart, M.D.,Bardwell, V.J.,Demeler, B.,Hart, P.J.,Kim, C.A.
Structure of the Polycomb Group Protein PCGF1 in Complex with BCOR Reveals Basis for Binding Selectivity of PCGF Homologs.
Structure, 21:665-671, 2013
Cited by
PubMed Abstract: Polycomb-group RING finger homologs (PCGF1, PCGF2, PCGF3, PCGF4, PCGF5, and PCGF6) are critical components in the assembly of distinct Polycomb repression complex 1 (PRC1)-related complexes. Here, we identify a protein interaction domain in BCL6 corepressor, BCOR, which binds the RING finger- and WD40-associated ubiquitin-like (RAWUL) domain of PCGF1 (NSPC1) and PCGF3 but not of PCGF2 (MEL18) or PCGF4 (BMI1). Because of the selective binding, we have named this domain PCGF Ub-like fold discriminator (PUFD). The structure of BCOR PUFD bound to PCGF1 reveals that (1) PUFD binds to the same surfaces as observed for a different Polycomb group RAWUL domain and (2) the ability of PUFD to discriminate among RAWULs stems from the identity of specific residues within these interaction surfaces. These data show the molecular basis for determining the binding preference for a PCGF homolog, which ultimately helps determine the identity of the larger PRC1-like assembly.
PubMed: 23523425
DOI: 10.1016/j.str.2013.02.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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