{"title":"一种新型折叠结构域的碱性亮氨酸拉链蛋白的DNA结合。","authors":"S Sato, K Makino, T Morii","doi":"10.1093/nass/44.1.13","DOIUrl":null,"url":null,"abstract":"<p><p>DNA-binding proteins frequently utilize short alpha-helices as their critical DNA recognition elements. In this research, we have employed the structure-based design to construct a small domain that could target the specific DNA sequences recognized by the yeast transcriptional activator GCN4. The new DNA binding motif recognizes specific DNA sequences as a dimer with high affinity and specificity under the physiological conditions.</p>","PeriodicalId":19394,"journal":{"name":"Nucleic acids symposium series","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/44.1.13","citationCount":"0","resultStr":"{\"title\":\"DNA binding of a basic leucine-zipper protein with novel folding domain.\",\"authors\":\"S Sato, K Makino, T Morii\",\"doi\":\"10.1093/nass/44.1.13\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>DNA-binding proteins frequently utilize short alpha-helices as their critical DNA recognition elements. In this research, we have employed the structure-based design to construct a small domain that could target the specific DNA sequences recognized by the yeast transcriptional activator GCN4. The new DNA binding motif recognizes specific DNA sequences as a dimer with high affinity and specificity under the physiological conditions.</p>\",\"PeriodicalId\":19394,\"journal\":{\"name\":\"Nucleic acids symposium series\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1093/nass/44.1.13\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nucleic acids symposium series\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1093/nass/44.1.13\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleic acids symposium series","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/nass/44.1.13","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
DNA binding of a basic leucine-zipper protein with novel folding domain.
DNA-binding proteins frequently utilize short alpha-helices as their critical DNA recognition elements. In this research, we have employed the structure-based design to construct a small domain that could target the specific DNA sequences recognized by the yeast transcriptional activator GCN4. The new DNA binding motif recognizes specific DNA sequences as a dimer with high affinity and specificity under the physiological conditions.
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