|
Sci. STKE, 22 April 2003 REVIEWSThe Structure and Function of Proline Recognition DomainsAli 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. 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). The editors suggest the following Related Resources on Science sites:In Science Signaling
In Science Magazine
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
|
Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)
Magazine | News | Signaling | Careers | Multimedia | Collections | Help | Site Map | RSS
Subscribe | Feedback | Privacy / Legal | About Us | Advertise With Us | Contact Us
© 2003 American Association for the Advancement of Science. All Rights Reserved.
AAAS is a partner of HINARI, AGORA, PatientInform, CrossRef, and COUNTER.
You have reached the bottom of the page. Back to top