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3IXS

Ring1B C-terminal domain/RYBP C-terminal domain Complex

Summary for 3IXS
Entry DOI10.2210/pdb3ixs/pdb
Related3GS2
DescriptorE3 ubiquitin-protein ligase RING2, RING1 and YY1-binding protein, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsring1b, rybp, polycomb, e3-ligase, chromosomal protein, transcription regulation, chromatin regulator, transcription repressor, ligase, metal-binding, nucleus, phosphoprotein, repressor, transcription, ubl conjugation pathway, zinc-finger, apoptosis, dna-binding, protein binding
Biological sourceHomo sapiens (human)
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Cellular locationNucleus (By similarity): Q99496
Nucleus: Q8N488
Total number of polymer chains12
Total formula weight100786.96
Authors
Wang, R.,Taylor, A.B.,Kim, C.A. (deposition date: 2009-09-04, release date: 2010-08-25, Last modification date: 2024-02-21)
Primary citationWang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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