3FM0
Crystal structure of WD40 protein Ciao1
Summary for 3FM0
Entry DOI | 10.2210/pdb3fm0/pdb |
Descriptor | Protein CIAO1, SULFATE ION (3 entities in total) |
Functional Keywords | wdr39, sgc, wd40, ciao1, nucleus, wd repeat, biosynthetic protein, structural genomics, structural genomics consortium |
Biological source | Homo sapiens |
Total number of polymer chains | 1 |
Total formula weight | 38803.86 |
Authors | Dong, A.,Ravichandran, M.,Crombet, L.,Cossar, D.,Edwards, A.M.,Arrowsmith, C.H.,Weigelt, J.,Bountra, C.,Bochkarev, A.,Min, J.,Ouyang, H.,Structural Genomics Consortium (SGC) (deposition date: 2008-12-19, release date: 2009-02-10, 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 Cited by 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: 21468892DOI: 10.1007/s13238-011-1018-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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