Competitive Binding of Proline-Rich Sequences by SH3, WW, and Other Functionally Related Protein Domains
作者： Marius Sudol , Mark T. Bedford
关键词:
摘要: Protein domains or modules are families of small (35 to 100 amino acids), conserved globular folds that bind DNA, RNA, phosphoinositides, and protein motifs (≈10 acids). A subset at least five different domain types possesses the ability proline-rich sequences; these include SH3, WW, EVH1, GYF, UEV domains. Some recognize same overlapping motifs, thus generating competitive pressure for motif binding. In addition, phosphorylation methylation residues within a can regulate Here, we highlight which likely compete ligands, how some interactions regulated by posttranslational modifications.
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Andrea Musacchio, How SH3 domains recognize proline Advances in Protein Chemistry. ,vol. 61, pp. 211- 268 ,(2002) , 10.1016/S0065-3233(02)61006-X
Jonathan D. Gary, Steven Clarke, RNA and Protein Interactions Modulated by Protein Arginine Methylation Progress in Nucleic Acid Research and Molecular Biology. ,vol. 61, pp. 65- 131 ,(1998) , 10.1016/S0079-6603(08)60825-9
A.E. Hagerman, L.G. Butler, The specificity of proanthocyanidin-protein interactions. Journal of Biological Chemistry. ,vol. 256, pp. 4494- 4497 ,(1981) , 10.1016/S0021-9258(19)69462-7
D. C. Chan, M. T. Bedford, P. Leder, Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. The EMBO Journal. ,vol. 15, pp. 1045- 1054 ,(1996) , 10.1002/J.1460-2075.1996.TB00442.X
Nicole M. Mahoney, Denise A. Rozwarski, Elena Fedorov, Alexander A. Fedorov, Steven C. Almo, Profilin binds proline-rich ligands in two distinct amide backbone orientations. Nature Structural & Molecular Biology. ,vol. 6, pp. 666- 671 ,(1999) , 10.1038/10722
Xin Huang, Florence Poy, Rongguang Zhang, Andrzej Joachimiak, Marius Sudol, Michael J. Eck, Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. Nature Structural & Molecular Biology. ,vol. 7, pp. 634- 638 ,(2000) , 10.1038/77923
B.J. Mayer, SH3 domains: complexity in moderation Journal of Cell Science. ,vol. 114, pp. 1253- 1263 ,(2001) , 10.1242/JCS.114.7.1253
Brian K. Kay, Michael P. Williamson, Marius Sudol, The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains The FASEB Journal. ,vol. 14, pp. 231- 241 ,(2000) , 10.1096/FASEBJ.14.2.231
Christian Freund, Gerhard Wagner, Volker Dötsch, Kazuhisa Nishizawa, Ellis L. Reinherz, The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nature Structural & Molecular Biology. ,vol. 6, pp. 656- 660 ,(1999) , 10.1038/10712
D Anderson, C. Koch, L Grey, C Ellis, M. Moran, T Pawson, Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors Science. ,vol. 250, pp. 979- 982 ,(1990) , 10.1126/SCIENCE.2173144