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- W156779433 abstract "Research Article1 February 1992free access Immunoglobulin VH clan and family identity predicts variable domain structure and may influence antigen binding. P.M. Kirkham P.M. Kirkham Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author F. Mortari F. Mortari Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author J.A. Newton J.A. Newton Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author H.W. Schroeder Jr H.W. Schroeder Jr Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author P.M. Kirkham P.M. Kirkham Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author F. Mortari F. Mortari Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author J.A. Newton J.A. Newton Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author H.W. Schroeder Jr H.W. Schroeder Jr Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. Search for more papers by this author Author Information P.M. Kirkham1, F. Mortari1, J.A. Newton1 and H.W. Schroeder1 1Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294. The EMBO Journal (1992)11:603-609https://doi.org/10.1002/j.1460-2075.1992.tb05092.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Mammalian immunoglobulin VH families can be grouped into three distinct clans based upon sequence conservation in two of the three framework (FR) intervals. Through replacement/silent site substitution analysis, molecular modeling and mathematical evaluation of known immunoglobulin crystal structures, we demonstrate that this conservation reflects preservation of protein sequence and structure. Each clan contains a characteristic FR 1 interval that is solvent-exposed and structurally separated from the antigen binding site. Families within a clan contain their own unique FR 3 interval that is capable of either influencing the conformation of the antigen binding site or interacting directly with antigen. Our results provide a structural context for theories that address differential use of VH families in the immune response. Previous ArticleNext Article Volume 11Issue 21 February 1992In this issue RelatedDetailsLoading ..." @default.
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- W156779433 title "Immunoglobulin VH clan and family identity predicts variable domain structure and may influence antigen binding." @default.
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