Qi Zheng, Wan-Ming Yang, Wen-Hao Yu, Bin Cai, Xin-Chen Teng, Yi Xie, Hong-Zhe Sun, Ming-Jie Zhang, Zhong-Xian Huang
{"title":"EAAEAE插入物对人金属硫蛋白-3性质的影响。","authors":"Qi Zheng, Wan-Ming Yang, Wen-Hao Yu, Bin Cai, Xin-Chen Teng, Yi Xie, Hong-Zhe Sun, Ming-Jie Zhang, Zhong-Xian Huang","doi":"10.1093/protein/gzg127","DOIUrl":null,"url":null,"abstract":"<p><p>MT3 shows apparently different properties and function from MT1 even though they have 70% sequence homology. Possibly the two inserts, Thr5 and a negatively charged hexapeptide at position-55 in MT3, play important roles. A series of MT3 variants around the EAAEAE hexapeptide have been prepared by site-directed mutagenesis and their properties and reactivity towards pH, EDTA and DTNB have been studied. Our detailed studies revealed that the EAAEAE insert is essential to the property of MT3. It is the hexapeptide insert, to some extent, making the MT3 alpha-domain looser and lower stability of the metal-thiolate cluster, which could be accessed more easily.</p>","PeriodicalId":20902,"journal":{"name":"Protein engineering","volume":"16 12","pages":"865-70"},"PeriodicalIF":0.0000,"publicationDate":"2003-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/protein/gzg127","citationCount":"23","resultStr":"{\"title\":\"The effect of the EAAEAE insert on the property of human metallothionein-3.\",\"authors\":\"Qi Zheng, Wan-Ming Yang, Wen-Hao Yu, Bin Cai, Xin-Chen Teng, Yi Xie, Hong-Zhe Sun, Ming-Jie Zhang, Zhong-Xian Huang\",\"doi\":\"10.1093/protein/gzg127\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>MT3 shows apparently different properties and function from MT1 even though they have 70% sequence homology. Possibly the two inserts, Thr5 and a negatively charged hexapeptide at position-55 in MT3, play important roles. A series of MT3 variants around the EAAEAE hexapeptide have been prepared by site-directed mutagenesis and their properties and reactivity towards pH, EDTA and DTNB have been studied. Our detailed studies revealed that the EAAEAE insert is essential to the property of MT3. It is the hexapeptide insert, to some extent, making the MT3 alpha-domain looser and lower stability of the metal-thiolate cluster, which could be accessed more easily.</p>\",\"PeriodicalId\":20902,\"journal\":{\"name\":\"Protein engineering\",\"volume\":\"16 12\",\"pages\":\"865-70\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1093/protein/gzg127\",\"citationCount\":\"23\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Protein engineering\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1093/protein/gzg127\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/protein/gzg127","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The effect of the EAAEAE insert on the property of human metallothionein-3.
MT3 shows apparently different properties and function from MT1 even though they have 70% sequence homology. Possibly the two inserts, Thr5 and a negatively charged hexapeptide at position-55 in MT3, play important roles. A series of MT3 variants around the EAAEAE hexapeptide have been prepared by site-directed mutagenesis and their properties and reactivity towards pH, EDTA and DTNB have been studied. Our detailed studies revealed that the EAAEAE insert is essential to the property of MT3. It is the hexapeptide insert, to some extent, making the MT3 alpha-domain looser and lower stability of the metal-thiolate cluster, which could be accessed more easily.