Structural implications of sequence variability in immunoglobulins.
Immunoglobulin sequences were compared by using a technique that takes into account the dissimilarity in physicochemical properties of amino acids. Exterior residues showed greater structural variability than interior residues. High structural variability was found at positions known from crystallographic studies to be involved in hapten binding.
D000595:Amino Acid Sequence; D000818:Animals; D014644:Genetic Variation; D006801:Humans; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007135:Immunoglobulin Variable Region; D007136:Immunoglobulins; D011817:Rabbits / Q000276:immunology; D051381:Rats / Q000276:immunology; D013045:Species Specificity
D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007135:Immunoglobulin Variable Region; D007136:Immunoglobulins