| Somatic mutations in immunoglobulin V gene determine the structure and function of the protein - an evidence from homology modeling | |
Abstract/OtherAbstract
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The antigen binding site of IgG immunoglobulins consists of two separate peptide domains,VH and VL. This part of combined domains contains three loops in each and it provides unique structure to distinguish antigens. The unique sequences encode the antigen binding site are determined by recombination of V region genes in both VH and VL during the differentiation of B-lymphocyte and successive somatic mutations. To investigate the correlation between the site of somatic hypermutations in immunoglobulin V region genes and the affinity maturation of antibodies, single clone derived anti-double stranded DNA antibody-producing hybridomas showing different DNA-binding activities were selected from an autoimmune disease-prone, (NZB x NZW)F1 female mouse. DNA sequence analyses showed that mutational points in V region genes were distributed in both complementality determining regions (CDRs) and framework regions and that there were no common mutational positions that account for the affinity m... |
Authors
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Junko Shimura,Satoru Miyazaki,Sachiko Hirose,Toshikazu Shirai,Hideaki Sugawara |
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Contributors
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The Pennsylvania State University CiteSeer Archives |
Publication Detail
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Publisher : unknown Type : - Format : ps |
Date Detail
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1995-11-27 |
Subject
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Junko Shimura,Satoru Miyazaki,Sachiko Hirose,Toshikazu Shirai,Hideaki Sugawara Somatic mutations in immunoglobulin V gene determine the structure and function of the protein - an evidence from homology modeling |
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Source
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http://www.cgl.ucsf.edu/psb/psb96/proceedings/shimura.ps |
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unrestricted |
Other Details
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Languages : en |
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