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Phylogenetic, Structural and Functional Relationships between WD- and Kelch-Repeat Proteins

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The Coronin Family of Proteins

Part of the book series: Subcellular Biochemistry ((SCBI,volume 48))

Abstract

The β-propeller domain is a widespread protein organizational motif. Typically, β-propeller proteins are encoded by repeated sequences where each repeat unit corresponds to a twisted β-sheet structural motif; these β-sheets are arranged in a circle around a central axis to generate the β-propeller structure. Two superfamilies of β-propeller proteins, the WD-repeat and Kelch-repeat families, exhibit similarities not only in structure, but, remarkably, also in the types of molecular functions they perform. While it is unlikely that WD and Kelch repeats evolved from a common ancestor, their evolution into diverse families of similar function may reflect the evolutionary advantages of the stable core β-propeller fold. In this chapter, we examine the relationships between these two widespread protein families, emphasizing recently published work relating to the structure and fucntion of both Kelch and WD-repeat proteins.

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Authors and Affiliations

  1. Department of Genetics, Yale University School of Medicine, 333 Cedar St, New Haven, CT, 06520, USA

    Andrew M. Hudson & Lynn Cooley

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  1. Andrew M. Hudson
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  2. Lynn Cooley
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Correspondence to Lynn Cooley .

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Editors and Affiliations

  1. Center for Biochemistry, University of Cologne, Cologne, Germany

    Christoph S. Clemen MD  & Ludwig Eichinger PhD  & 

  2. The Scripps Research Institute, La Jolla, California, USA

    Vasily Rybakin PhD

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Hudson, A.M., Cooley, L. (2008). Phylogenetic, Structural and Functional Relationships between WD- and Kelch-Repeat Proteins. In: Clemen, C.S., Eichinger, L., Rybakin, V. (eds) The Coronin Family of Proteins. Subcellular Biochemistry, vol 48. Springer, New York, NY. https://doi.org/10.1007/978-0-387-09595-0_2

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