{"title":"人和小鼠低亲和力Fc epsilon受体(Fc epsilon RII/CD23)凝集素同源结构域的建模。","authors":"E A Padlan, B A Helm","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Models of the lectin-homology domains of the human and murine low-affinity receptors for IgE (Fc epsilon RII/CD23) were built on the basis of sequence similarity with rat mannose-binding protein, the structure of which is known. The sites on Fc epsilon RII/CD23 that are possibly involved in the interaction with IgE and with another ligand, CD21/CR2, are proposed. The models may assist the design of protein engineering experiments for the study of the reactivity of these molecules.</p>","PeriodicalId":21112,"journal":{"name":"Receptor","volume":"3 4","pages":"325-41"},"PeriodicalIF":0.0000,"publicationDate":"1993-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23).\",\"authors\":\"E A Padlan, B A Helm\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Models of the lectin-homology domains of the human and murine low-affinity receptors for IgE (Fc epsilon RII/CD23) were built on the basis of sequence similarity with rat mannose-binding protein, the structure of which is known. The sites on Fc epsilon RII/CD23 that are possibly involved in the interaction with IgE and with another ligand, CD21/CR2, are proposed. The models may assist the design of protein engineering experiments for the study of the reactivity of these molecules.</p>\",\"PeriodicalId\":21112,\"journal\":{\"name\":\"Receptor\",\"volume\":\"3 4\",\"pages\":\"325-41\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1993-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Receptor\",\"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":"Receptor","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23).
Models of the lectin-homology domains of the human and murine low-affinity receptors for IgE (Fc epsilon RII/CD23) were built on the basis of sequence similarity with rat mannose-binding protein, the structure of which is known. The sites on Fc epsilon RII/CD23 that are possibly involved in the interaction with IgE and with another ligand, CD21/CR2, are proposed. The models may assist the design of protein engineering experiments for the study of the reactivity of these molecules.