Variable Region Sequences of Five Human Immunoglobulin Heavy Chains of the VHIII Subgroup: Definitive Identification of Four Heavy Chain Hypervariable Regions

The variable regions of five human immunoglobulin heavy chains of the VHIII subgroup have been totally sequenced. Three of the heavy chains belonged to the IgG class and two to the IgA class. Examination of these sequences, and comparison with additional published heavy chain sequences, showed that...

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Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 71; no. 3; pp. 845 - 848
Main Authors Capra, J. Donald, Kehoe, J. Michael
Format Journal Article
LanguageEnglish
Published National Academy of Sciences of the United States of America 01.03.1974
National Acad Sciences
Subjects
Amino acids
Antibodies
Binding sites
Biological Sciences: Immunology
Bromides
Globulins
Immunoglobulin heavy chains
Immunoglobulins
Molecules
Myeloma proteins
Proteins
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Summary:The variable regions of five human immunoglobulin heavy chains of the VHIII subgroup have been totally sequenced. Three of the heavy chains belonged to the IgG class and two to the IgA class. Examination of these sequences, and comparison with additional published heavy chain sequences, showed that a total of four hypervariable regions is characteristic of human heavy chain variable regions. The relatively conserved character of large segments of the heavy chain variable region was very evident in these studies. The conserved segments, which are those sections located outside the hypervariable regions, comprise approximately 65% of the total heavy chain variable region. The following general structural pattern for antibody molecules emerges from this and related studies: an overall combining region superstructure is provided by the more conserved segments while the refinements of the active site specificity are a function of hypervariable regions.
ISSN:0027-8424
1091-6490