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We analyzed the substrate specificities of wild\u2010type v\u2010Src and the mutants using two series of peptides that varied at residues C\u2010terminal to tyrosine. The peptides contained either the YMTM motif found in insulin receptor substrate\u20101 (IRS\u20101) or the YGEF motif identified from peptide library experiments to be the optimal sequence for Src. Mutations at positions Leu\u2010472 or Thr\u2010429 caused changes in substrate specificity at positions P+1 and P+3 (i.e. one or three residues C\u2010terminal to tyrosine). This was particularly evident in the case of the L\u2010472W mutant, which had pronounced alterations in its preferences at the P+1 position. The results suggest that residue Leu\u2010472 plays a role in P+1 substrate recognition by Src. We discuss the results in the light of recent work on the roles of the SH2, SH3 and catalytic domains of Src in substrate specificity.<\/jats:p>","DOI":"10.1016\/s0014-5793(99)00992-8","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T15:03:33Z","timestamp":1027609413000},"page":"403-408","source":"Crossref","is-referenced-by-count":14,"title":["Identification of residues involved in v\u2010Src substrate recognition by site\u2010directed mutagenesis"],"prefix":"10.1002","volume":"456","author":[{"given":"Noriko","family":"Yokoyama","sequence":"first","affiliation":[]},{"given":"W.Todd","family":"Miller","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[1999,8,11]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0304-419X(96)00003-0"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/373573a0"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(93)90634-3"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/385595a0"},{"key":"e_1_2_5_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/385602a0"},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/385650a0"},{"key":"e_1_2_5_8_1","doi-asserted-by":"publisher","DOI":"10.1038\/373536a0"},{"key":"e_1_2_5_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.25.15325"},{"key":"e_1_2_5_10_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.14.5.2883"},{"key":"e_1_2_5_11_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/16.18.5572"},{"key":"e_1_2_5_12_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.4.1579"},{"key":"e_1_2_5_13_1","doi-asserted-by":"publisher","DOI":"10.1038\/367375a0"},{"key":"e_1_2_5_14_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.8.4995"},{"key":"e_1_2_5_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)74581-5"},{"key":"e_1_2_5_16_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00225883"},{"key":"e_1_2_5_17_1","unstructured":"Atherton E. and Sheppard R.C. 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