Thu, 24 Jul 2008 20:12:48 BST CiteULike: neils Reményi http://www.citeulike.org/user/neils/author/Reményi CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/neils/article/2054454 <i>Curr Opin Struct Biol, Vol. 16, No. 6. (Dec 2006), pp. 676-685.</i><br /><br />To achieve high biological specificity, protein kinases and phosphatases often recognize their targets through interactions that occur outside of the active site. Although the role of modular protein-protein interaction domains in kinase and phosphatase signaling has been well characterized, it is becoming clear that many kinases and phosphatases utilize docking interactions - recognition of a short peptide motif in target partners by a groove on the catalytic domain that is separate from the active site. Docking is particularly prevalent in serine/threonine kinases and phosphatases, and is a versatile organizational tool for building complex signaling networks; it confers a high degree of specificity and, in some cases, allosteric regulation. Docking interactions in protein kinase and phosphatase networks. Attila Reményi Matthew Good Wendell Lim Curr Opin Struct Biol, Vol. 16, No. 6. (Dec 2006), pp. 676-685. 2007-12-04T03:22:10-00:00 2006 Curr Opin Struct Biol 16 6 676 685 allosteric article-predikin binding biological complex conformation design drug kinase map models molecular multiprotein phosphatase phosphoprotein protein regulation signal signaling sites structure system tertiary transduction