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Sci. STKE, 22 April 2003
Vol. 2003, Issue 179, p. re8
[DOI: 10.1126/scisignal.1792003re8]

REVIEWS

The Structure and Function of Proline Recognition Domains

Ali Zarrinpar1,2, 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.

*Corresponding author. Telephone, 415-502-8080; fax, 415-514-4242; e-mail: wlim{at}itsa.ucsf.edu

Citation: A. Zarrinpar, R. P. Bhattacharyya, W. A. Lim, The Structure and Function of Proline Recognition Domains. Sci. STKE 2003, re8 (2003).

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