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MLRS 242 Immunology Pat Reed Antibodies. Serum proteins. General antibody structure. Enzyme digestion fragments. Protein structure of immunoglobulins. Early amino acid sequence experiments were unsuccessful—too much variation Multiple myeloma serum is 95% same antibody
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Protein structure of immunoglobulins • Early amino acid sequence experiments were unsuccessful—too much variation • Multiple myeloma serum is 95% same antibody • Bence-jones protein found in urine of myeloma patients is excess light chain • 110 amino acids highly variable, rest are quite constant • 5 different isotypes identified: based on type of heavy chain: G,D,E,M,A • Human light chains: 60% kappa (K) chains, 40% lambda (L) chains
Ribbon model of variable region • Variable region contains highly variable connecting regions called complementarity-determining regions or CDRs • These regions are also shown to be the antigen binding sites
Amino acid diversity of variable domains – complementarity- determining regions (CDRs)
Hiv protease and Fab fragmentConformational change in Fab domain
Isotype – different species • Allotype – same species, different alleles • Idiotype – same species, different VH and VL domains
Isotypic determinants – different species variation within the constant region
Allotypic determinants – different constant regions within the same species – different alleles
Idiotypic determinants – variations in the variable region within the same antibody type
Immunoglobulin superfamily of cell receptors – evolved from common ancestor gene