V S Khristophorov, D A Prokhorov, M A Timchenko, Iu A Kudrevatykh, L V Gushchina, V V Filimonov, V P Kutyshenko
{"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}
引用次数: 0
Abstract
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.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
