3GS2

Ring1B C-terminal domain/Cbx7 Cbox Complex

Summary for 3GS2

• Entry DOI: 10.2210/pdb3gs2/pdb
• Descriptor: E3 ubiquitin-protein ligase RING2, Chromobox protein homolog 7, SULFATE ION, ... (5 entities in total)
• Functional Keywords: ring1b, cbox, cbx7, polycomb, e3-ligase, chromosomal protein, transcription regulation, chromatin regulator, transcription repressor, ligase, metal-binding, nucleus, phosphoprotein, repressor, transcription, ubl conjugation pathway, zinc-finger
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus (By similarity): Q99496; Nucleus: O95931
• Total number of polymer chains: 4
• Total formula weight: 32157.17

Authors

Wang, R.,Taylor, A.B.,Kim, C.A. (deposition date: 2009-03-26, release date: 2010-08-25, Last modification date: 2024-02-21)

Primary citation

Wang, R.,Taylor, A.B.,Leal, B.Z.,Chadwell, L.V.,Ilangovan, U.,Robinson, A.K.,Schirf, V.,Hart, P.J.,Lafer, E.M.,Demeler, B.,Hinck, A.P.,McEwen, D.G.,Kim, C.A.
Polycomb Group Targeting through Different Binding Partners of RING1B C-Terminal Domain.
Structure, 18:966-975, 2010

PubMed Abstract: RING1B, a Polycomb Group (PcG) protein, binds methylated chromatin through its association with another PcG protein called Polycomb (Pc). However, RING1B can associate with nonmethylated chromatin suggesting an alternate mechanism for RING1B interaction with chromatin. Here, we demonstrate that two proteins with little sequence identity between them, the Pc cbox domain and RYBP, bind the same surface on the C-terminal domain of RING1B (C-RING1B). Pc cbox and RYBP each fold into a nearly identical, intermolecular beta sheet with C-RING1B and a loop structure which are completely different in the two proteins. Both the beta sheet and loop are required for stable binding and transcription repression. Further, a mutation engineered to disrupt binding on the Drosophila dRING1 protein prevents chromatin association and PcG function in vivo. These results suggest that PcG targeting to different chromatin locations relies, in part, on binding partners of C-RING1B that are diverse in sequence and structure.

PubMed: 20696397
DOI: 10.1016/j.str.2010.04.013

Experimental method

X-RAY DIFFRACTION (1.699 Å)