{"title":"人类酪氨酸酶基因错义突变在I型(酪氨酸酶相关)眼皮肤白化病中的非随机分布。","authors":"R A King, M M Mentink, W S Oetting","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Type I oculocutaneous albinism (OCA) is produced by mutations of the tyrosinase gene. We report four new missense mutations in the tyrosinase gene in patients with type IA OCA. Three of these mutations occur within exon I and the fourth mutation within exon IV. Analysis of the distribution of these four missense mutations and 12 previously reported missense mutations shows that most cluster in four areas of the gene. Two clusters involve the copper A and copper B binding sites and could disrupt the metal ion-protein interaction necessary for enzyme function. The other two clusters are in exon I and exon IV and could represent important functional domains of the enzyme. We conclude that analysis of the tyrosinase missense mutations will provide insight into the structure-function relationship of this enzyme.</p>","PeriodicalId":77573,"journal":{"name":"Molecular biology & medicine","volume":"8 1","pages":"19-29"},"PeriodicalIF":0.0000,"publicationDate":"1991-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism.\",\"authors\":\"R A King, M M Mentink, W S Oetting\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Type I oculocutaneous albinism (OCA) is produced by mutations of the tyrosinase gene. We report four new missense mutations in the tyrosinase gene in patients with type IA OCA. Three of these mutations occur within exon I and the fourth mutation within exon IV. Analysis of the distribution of these four missense mutations and 12 previously reported missense mutations shows that most cluster in four areas of the gene. Two clusters involve the copper A and copper B binding sites and could disrupt the metal ion-protein interaction necessary for enzyme function. The other two clusters are in exon I and exon IV and could represent important functional domains of the enzyme. We conclude that analysis of the tyrosinase missense mutations will provide insight into the structure-function relationship of this enzyme.</p>\",\"PeriodicalId\":77573,\"journal\":{\"name\":\"Molecular biology & medicine\",\"volume\":\"8 1\",\"pages\":\"19-29\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular biology & medicine\",\"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":"Molecular biology & medicine","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism.
Type I oculocutaneous albinism (OCA) is produced by mutations of the tyrosinase gene. We report four new missense mutations in the tyrosinase gene in patients with type IA OCA. Three of these mutations occur within exon I and the fourth mutation within exon IV. Analysis of the distribution of these four missense mutations and 12 previously reported missense mutations shows that most cluster in four areas of the gene. Two clusters involve the copper A and copper B binding sites and could disrupt the metal ion-protein interaction necessary for enzyme function. The other two clusters are in exon I and exon IV and could represent important functional domains of the enzyme. We conclude that analysis of the tyrosinase missense mutations will provide insight into the structure-function relationship of this enzyme.