Structural implications of sequence variability in immunoglobulins.

AUTOR(ES)

Padlan, E A

RESUMO

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.

Documentos Relacionados

• Variability of three-dimensional structure in immunoglobulins.
• Immunoglobulins.
• Somatic diversification of immunoglobulins.
• Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins.
• Location and structural significance of the oligosaccharides in human Ig-A1 and IgA2 immunoglobulins.