3GFC

Crystal Structure of Histone-binding protein RBBP4

Summary for 3GFC

• Entry DOI: 10.2210/pdb3gfc/pdb
• Descriptor: Histone-binding protein RBBP4 (2 entities in total)
• Functional Keywords: rbbp4, histone-binding protein, structural genomics, structural genomics consortium, sgc, cell cycle, chromatin regulator, dna replication, nucleus, repressor, transcription, transcription regulation, wd repeat
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q09028
• Total number of polymer chains: 1
• Total formula weight: 47709.53

Authors

Amaya, M.F.,Dong, A.,Li, Z.,He, H.,Ni, S.,Edwards, A.M.,Arrowsmith, C.H.,Weigelt, J.,Bountra, C.,Bochkarev, A.,Min, J.,Ouyang, H.,Structural Genomics Consortium (SGC) (deposition date: 2009-02-26, release date: 2009-04-14, Last modification date: 2023-09-06)

Primary citation

Xu, C.,Min, J.
Structure and function of WD40 domain proteins.
Protein Cell, 2:202-214, 2011

PubMed Abstract: The WD40 domain exhibits a β-propeller architecture, often comprising seven blades. The WD40 domain is one of the most abundant domains and also among the top interacting domains in eukaryotic genomes. In this review, we will discuss the identification, definition and architecture of the WD40 domains. WD40 domain proteins are involved in a large variety of cellular processes, in which WD40 domains function as a protein-protein or protein-DNA interaction platform. WD40 domain mediates molecular recognition events mainly through the smaller top surface, but also through the bottom surface and sides. So far, no WD40 domain has been found to display enzymatic activity. We will also discuss the different binding modes exhibited by the large versatile family of WD40 domain proteins. In the last part of this review, we will discuss how post-translational modifications are recognized by WD40 domain proteins.

PubMed: 21468892
DOI: 10.1007/s13238-011-1018-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)