4HPL

PCGF1 Ub fold (RAWUL)/BCOR PUFD Complex

Summary for 4HPL

• Entry DOI: 10.2210/pdb4hpl/pdb
• Related: 4HPM
• Descriptor: BCL-6 corepressor, Polycomb group RING finger protein 1 (3 entities in total)
• Functional Keywords: polycomb, bcor, bcl-6 co-repressor, 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 source: Homo sapiens (human); More
• Cellular location: Nucleus: Q6W2J9 Q9BSM1
• Total number of polymer chains: 2
• Total formula weight: 24753.55

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: 2024-02-28)

Primary citation

Junco, 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

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

Experimental method

X-RAY DIFFRACTION (2 Å)