Structural repertoire in human V{sub L} pseudogenes of immunoglobulins: Comparison with functional germline genes and amino acid sequences
- Universidad Veracruzana, Veracruz, MX (United States); and others
Antibody molecules are highly antigen-specific receptors of the immune system. Antigen-antibody interaction involves the antibody V{sub L} and V{sub H} domains, each composed of a framework whose structure is well conserved. The antigen-binding site is composed of six hypervariable loops, three from the V{sub L} domain and three from the V{sub H} domain: L1, L2, L3, and H1, H2, H3, respectively. Genetically, L1 and L2 are encoded by the V{sub L} gene, while L3 is produced by the recombination of an additional gene segment, A. In a similar way, H1 and H2 are encoded by the V{sub H} gene, and H3 is a result of the recombination of two additional gene segments, D and J{sub H}. Analysis of antibodies of known atomic structure has revealed a small number of main-chain conformations or canonical structures for L1, L2, and L3, as well as for H1 and H2. Canonical structures in five of six hypervariable loops imply that only a few main-chain conformations are present in a large set of antibody molecules with different loop sequences. Examination of the known human IGHV, IGKV, and IGLV functional germline genes indicates that most of these sequences have canonical structures. This finding provides evidence concerning structural restrictions at work in the process of antigen recognition. 28 refs., 1 fig., 4 tabs.
- OSTI ID:
- 240998
- Journal Information:
- Immunogenetics, Vol. 43, Issue 1-2; Other Information: PBD: 1996
- Country of Publication:
- United States
- Language:
- English
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