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The structure of the RbBP5 β-propeller domain reveals a surface with potential nucleic acid binding sites

DOI: 10.1093/nar/gky199 DOI Help

Authors: Anshumali Mittal (The Francis Crick Institute) , Fruzsina Hobor (University College London) , Ying Zhang (The Francis Crick Institute) , Stephen R. Martin (The Francis Crick Institute) , Steven J. Gamblin (The Francis Crick Institute) , Andres Ramos (University College London) , Jon Wilson (The Francis Crick Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research , VOL 447

State: Published (Approved)
Published: March 2018
Diamond Proposal Number(s): 9826

Open Access Open Access

Abstract: The multi-protein complex WRAD, formed by WDR5, RbBP5, Ash2L and Dpy30, binds to the MLL SET domain to stabilize the catalytically active conformation required for histone H3K4 methylation. In addition, the WRAD complex contributes to the targeting of the activated complex to specific sites on chromatin. RbBP5 is central to MLL catalytic activation, by making critical contacts with the other members of the complex. Interestingly its only major structural domain, a canonical WD40 repeat β-propeller, is not implicated in this function. Here, we present the structure of the RbBP5 β-propeller domain revealing a distinct, feature rich surface, dominated by clusters of Arginine residues. Our nuclear magnetic resonance binding data supports the hypothesis that in addition to the role of RbBP5 in catalytic activation, its β-propeller domain is a platform for the recruitment of the MLL complexes to chromatin targets through its direct interaction with nucleic acids.

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography

Added On: 05/04/2018 10:45


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)