Docking interactions in protein kinase and phosphatase networks.

@article{Remenyi2006, abstract = {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.}, author = {Rem\'{e}nyi, Attila and Good, Matthew C. and Lim, Wendell A. }, citeulike-article-id = {2054454}, doi = {10.1016/j.sbi.2006.10.008}, journal = {Curr Opin Struct Biol}, keywords = {allosteric, article-predikin, binding, biological, complexes, conformation, design, drug, kinase, kinases, map, models, molecular, multiprotein, phosphatases, phosphoprotein, protein, regulation, signal, signaling, sites, structure, system, tertiary, transduction}, month = {Dec}, number = {6}, pages = {676--685}, posted-at = {2007-12-04 03:22:14}, priority = {2}, title = {Docking interactions in protein kinase and phosphatase networks.}, url = {http://dx.doi.org/10.1016/j.sbi.2006.10.008}, volume = {16}, year = {2006} }

TY - JOUR ID - Remenyi2006 TI - Docking interactions in protein kinase and phosphatase networks. JF - Curr Opin Struct Biol VL - 16 IS - 6 SP - 676 EP - 685 N2 - 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. KW - allosteric KW - article-predikin KW - binding KW - biological KW - complexes KW - conformation KW - design KW - drug KW - kinase KW - kinases KW - map KW - models KW - molecular KW - multiprotein KW - phosphatases KW - phosphoprotein KW - protein KW - regulation KW - signal KW - signaling KW - sites KW - structure KW - system KW - tertiary KW - transduction AU - Reményi, Attila AU - Good, Matthew AU - Lim, Wendell PY - 2006/Dec// UR - http://dx.doi.org/10.1016/j.sbi.2006.10.008 ER -