Surya V S R K Pulavarti, Yuanpeng J Huang, Kari Pederson, Thomas B Acton, Rong Xiao, John K Everett, James H Prestegard, Gaetano T Montelione, Thomas Szyperski
{"title":"免疫球蛋白样结构域7和12的溶液核磁共振结构有助于人类癌症蛋白相互作用网络的结构覆盖。","authors":"Surya V S R K Pulavarti, Yuanpeng J Huang, Kari Pederson, Thomas B Acton, Rong Xiao, John K Everett, James H Prestegard, Gaetano T Montelione, Thomas Szyperski","doi":"10.1007/s10969-014-9185-y","DOIUrl":null,"url":null,"abstract":"<p><p>High-quality solution NMR structures of immunoglobulin-like domains 7 and 12 from human obscurin-like protein 1 were solved. The two domains share 30% sequence identity and their structures are, as expected, rather similar. The new structures contribute to structural coverage of human cancer associated proteins. Mutations of Arg 812 in domain 7 cause the rare 3-M syndrome, and this site is located in a surface area predicted to be involved in protein-protein interactions.</p>","PeriodicalId":73957,"journal":{"name":"Journal of structural and functional genomics","volume":"15 4","pages":"209-14"},"PeriodicalIF":0.0000,"publicationDate":"2014-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s10969-014-9185-y","citationCount":"0","resultStr":"{\"title\":\"Solution NMR structures of immunoglobulin-like domains 7 and 12 from obscurin-like protein 1 contribute to the structural coverage of the Human Cancer Protein Interaction Network.\",\"authors\":\"Surya V S R K Pulavarti, Yuanpeng J Huang, Kari Pederson, Thomas B Acton, Rong Xiao, John K Everett, James H Prestegard, Gaetano T Montelione, Thomas Szyperski\",\"doi\":\"10.1007/s10969-014-9185-y\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>High-quality solution NMR structures of immunoglobulin-like domains 7 and 12 from human obscurin-like protein 1 were solved. The two domains share 30% sequence identity and their structures are, as expected, rather similar. The new structures contribute to structural coverage of human cancer associated proteins. Mutations of Arg 812 in domain 7 cause the rare 3-M syndrome, and this site is located in a surface area predicted to be involved in protein-protein interactions.</p>\",\"PeriodicalId\":73957,\"journal\":{\"name\":\"Journal of structural and functional genomics\",\"volume\":\"15 4\",\"pages\":\"209-14\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2014-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/s10969-014-9185-y\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of structural and functional genomics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/s10969-014-9185-y\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2014/7/3 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of structural and functional genomics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/s10969-014-9185-y","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2014/7/3 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
Solution NMR structures of immunoglobulin-like domains 7 and 12 from obscurin-like protein 1 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
High-quality solution NMR structures of immunoglobulin-like domains 7 and 12 from human obscurin-like protein 1 were solved. The two domains share 30% sequence identity and their structures are, as expected, rather similar. The new structures contribute to structural coverage of human cancer associated proteins. Mutations of Arg 812 in domain 7 cause the rare 3-M syndrome, and this site is located in a surface area predicted to be involved in protein-protein interactions.