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Structure and function of WD40 domain proteins.

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  • 1. Structural Genomics Consortium, University of Toronto, 101 College St., Toronto, Ontario, Canada.
      Authors
    • Xu C 1
    (1 author)

ORCIDs linked to this article

Protein & Cell, 01 Mar 2011, 2(3):202-214
https://doi.org/10.1007/s13238-011-1018-1 PMID: 21468892 PMCID: PMC4875305

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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.

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Protein Cell. 2011 Mar; 2(3): 202–214.
Published online 2011 Apr 6. https://doi.org/10.1007/s13238-011-1018-1
PMCID: PMC4875305
PMID: 21468892

Structure and function of WD40 domain proteins

Chao Xu1 and Jinrong Mincorresponding author1,2
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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.

Keywords: WD40, beta-propeller, protein-protein interaction, scaffold, post-translational modification

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Article citations

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Data 

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.

Funding 

Funders who supported this work.

Canadian Institutes of Health Research

    Wellcome Trust