4HPM : PCGF1 Ub fold (RAWUL)/BCORL1 PUFD Complex

  • Sarah E. Junco (Contributor)
  • Renjing Wang (Contributor)
  • John C. Gaipa (Contributor)
  • Alexander Bryan Taylor (Contributor)
  • Micah D. Gearhart (Contributor)
  • Vivian J. Bardwell (Contributor)
  • P. John Hart (VA Medical Center) (Contributor)
  • Chongwoo A. Kim (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2013-05-01
Deposition Date:2012-10-24
Revision Date:
Molecular Weight:50575.8
Macromolecule Type:Protein
Residue Count:430
Atom Site Count:3225

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.
Date made available2013

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