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Sci. STKE, 22 April 2003
Vol. 2003, Issue 179, p. re8
The Structure and Function of Proline Recognition Domains
Roby P. Bhattacharyya1,2, and
Wendell A. Lim2*
1Program in Biological Sciences, University of California San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA. 2Department of Cellular and Molecular Pharmacology and Department of Biochemistry and Biophysics, University of California San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.
Gloss: This STKE Review describes one class of protein interaction domains: the proline-binding domains. Conserved protein domains are critical to the assembly and regulation of many intracellular signaling complexes and pathways. Proline-binding domains serve two main functions: to serve as assembly points in signaling complexes and to serve a regulatory role in controlling protein activity. With seven figures and one table, this review provides detailed structural information about three main proline-binding motifs (the SH3, WW, and EVH1 domains), as well as brief descriptions of other proline-binding domains. The review has 91 references, seven figures, one table, and five interactive images.