Koichi Kato , Wolf H Fridman , Yoji Arata , Catherine Sautès-Fridman
{"title":"Fc的构象变化阻止了两个Fcγ受体分子与一个IgG的结合","authors":"Koichi Kato , Wolf H Fridman , Yoji Arata , Catherine Sautès-Fridman","doi":"10.1016/S0167-5699(00)01666-2","DOIUrl":null,"url":null,"abstract":"<div><p>Recent NMR analyses of IgG–FcγR interactions in solution have identified the FcγR-binding site on the Fc region and provided evidence for a conformational change in the Fc occurring during the interaction. Here, Koichi Kato and colleagues discuss how this conformational change explains the incapacity of IgG molecules to trigger responses deleterious to the organism, in the absence of antigen cross-linking.</p></div>","PeriodicalId":73346,"journal":{"name":"Immunology today","volume":"21 7","pages":"Pages 310-312"},"PeriodicalIF":0.0000,"publicationDate":"2000-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-5699(00)01666-2","citationCount":"29","resultStr":"{\"title\":\"A conformational change in the Fc precludes the binding of two Fcγ receptor molecules to one IgG\",\"authors\":\"Koichi Kato , Wolf H Fridman , Yoji Arata , Catherine Sautès-Fridman\",\"doi\":\"10.1016/S0167-5699(00)01666-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Recent NMR analyses of IgG–FcγR interactions in solution have identified the FcγR-binding site on the Fc region and provided evidence for a conformational change in the Fc occurring during the interaction. Here, Koichi Kato and colleagues discuss how this conformational change explains the incapacity of IgG molecules to trigger responses deleterious to the organism, in the absence of antigen cross-linking.</p></div>\",\"PeriodicalId\":73346,\"journal\":{\"name\":\"Immunology today\",\"volume\":\"21 7\",\"pages\":\"Pages 310-312\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0167-5699(00)01666-2\",\"citationCount\":\"29\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Immunology today\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0167569900016662\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Immunology today","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0167569900016662","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A conformational change in the Fc precludes the binding of two Fcγ receptor molecules to one IgG
Recent NMR analyses of IgG–FcγR interactions in solution have identified the FcγR-binding site on the Fc region and provided evidence for a conformational change in the Fc occurring during the interaction. Here, Koichi Kato and colleagues discuss how this conformational change explains the incapacity of IgG molecules to trigger responses deleterious to the organism, in the absence of antigen cross-linking.