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By binding with moderate affinity and selectivity to proline-rich ligands, these domains play critical roles in a wide variety of biological processes ranging from regulation of enzymes by intramolecular interactions, increasing the local concentration or altering the subcellular localization of components of signaling pathways, and mediating the assembly of large multiprotein complexes. SH3 domains and their binding sites have cropped up in many hundreds of proteins in species from yeast to man, which suggests that they provide the cell with an especially handy and adaptable means of bringing proteins together. The wealth of genetic, biochemical and structural information available provides an intimate and detailed portrait of the domain, serving as a framework for understanding other modular protein-interaction domains. Processes regulated by SH3 domains also raise important questions about the nature of specificity and the overall logic governing networks of protein interactions.<\/jats:p>","DOI":"10.1242\/jcs.114.7.1253","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T18:47:19Z","timestamp":1619376439000},"page":"1253-1263","source":"Crossref","is-referenced-by-count":691,"title":["SH3 domains: complexity in moderation"],"prefix":"10.1242","volume":"114","author":[{"given":"Bruce J.","family":"Mayer","sequence":"first","affiliation":[{"name":"University of Connecticut Health Center, 263 Farmington Avenue Department of Genetics and Developmental Biology , , Farmington, CT 06030-3301, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2001,4,1]]},"reference":[{"key":"2024011500513145500_JOCES_114_7_1253C1","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1038\/20726","article-title":"Structure of Cdc42 in complex with the GTPase-binding domain of the \u2018Wiskott-Aldrich syndrome\u2019 protein","volume":"399","author":"Abdul-Manan","year":"1999","journal-title":"Nature"},{"key":"2024011500513145500_JOCES_114_7_1253C2","doi-asserted-by":"publisher","first-page":"36472","DOI":"10.1074\/jbc.M005424200","article-title":"Abl family kinases and Cbl cooperate with the Nck adaptor to modulate Xenopus development","volume":"275","author":"Adler","year":"2000","journal-title":"J. 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