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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.

Abstract: One particularly abundant group of modular recognition domains consists of those that bind proline-rich motifs. Such modules, including the SH3, WW, and EVH1 domains, play a critical role in the assembly and regulation of many intracellular signaling complexes. These domains use strikingly similar molecular mechanisms of proline recognition. We discuss some of the potential biological advantages conferred by proline recognition, which may explain its widespread use in signaling.

*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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