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

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 chrom...

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Detalles Bibliográficos
Autores principales: Mittal, Anshumali, Hobor, Fruzsina, Zhang, Ying, Martin, Stephen R, Gamblin, Steven J, Ramos, Andres, Wilson, Jon R
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6283417/
https://www.ncbi.nlm.nih.gov/pubmed/29897600
http://dx.doi.org/10.1093/nar/gky199

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6283417/
https://www.ncbi.nlm.nih.gov/pubmed/29897600
http://dx.doi.org/10.1093/nar/gky199

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