V S Khristophorov, D A Prokhorov, M A Timchenko, Iu A Kudrevatykh, L V Gushchina, V V Filimonov, V P Kutyshenko
{"title":"[嵌合SHA-D结构域(“SH3-Bergerac”):溶液中的3d结构和动力学研究]。","authors":"V S Khristophorov, D A Prokhorov, M A Timchenko, Iu A Kudrevatykh, L V Gushchina, V V Filimonov, V P Kutyshenko","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Protein SHA-D of \"SH3-Bergerac\" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of \"SH3-Bergerac\" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile.</p>","PeriodicalId":9325,"journal":{"name":"Bioorganicheskaia khimiia","volume":"36 4","pages":"505-13"},"PeriodicalIF":0.0000,"publicationDate":"2010-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Chimeric SHA-D domain (\\\"SH3-Bergerac\\\"): 3D-structure and dynamics studies in solution].\",\"authors\":\"V S Khristophorov, D A Prokhorov, M A Timchenko, Iu A Kudrevatykh, L V Gushchina, V V Filimonov, V P Kutyshenko\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Protein SHA-D of \\\"SH3-Bergerac\\\" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of \\\"SH3-Bergerac\\\" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile.</p>\",\"PeriodicalId\":9325,\"journal\":{\"name\":\"Bioorganicheskaia khimiia\",\"volume\":\"36 4\",\"pages\":\"505-13\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2010-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioorganicheskaia khimiia\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioorganicheskaia khimiia","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Chimeric SHA-D domain ("SH3-Bergerac"): 3D-structure and dynamics studies in solution].
Protein SHA-D of "SH3-Bergerac" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of "SH3-Bergerac" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile.
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