Advances in Immunology, Vol. 20 by F.J. Dixon, Henry G. Kunkel (Eds.)

By F.J. Dixon, Henry G. Kunkel (Eds.)

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The authors postulate that one chain may actually assume the conformation of the heavy chain in an immunoglobulin molecule. The dimer has within its structure a definite cavity that the authors interpret as representing the antigen-binding site of an antibody molecule. This cavity is lined by residues that would correspond in position to the three hypervariable regions of the light chain. Two large side chains of residues 34 and 52 in both monomers protrude into the cavity. Thus, although this was a study on a Bence-Jones dimer, it provided many insights into the nature of the combining site, and the results were consistent with the notion that the hypervariable regions formed a portion of the site.

DONALD CAPRA AND J. , and Berek, C. (1973). Eur. J. Immunol. 3, 599. , and Kindt, T. J. (1971). J. Exp. Med. 134,532. Ely, K. , Girling, R. , Cunningham, D. , and Edmundson, A. B. ( 1973). Biochemistry 12,4233. , and Kabat, E. A. (1972). E x p . Med. 135, 1247. , Kabat, E. , and Marsh, W. L. ( 1971). J. Immunol. 106, 1578. , Kunkel, H. , and Roelke, D. (1974). Clin. E x p . Immunol. (in press). , Palm, W. , and Press, E. M. (1989). FEBS (Fed. Eur. Biochem. ) Lett. 5, 20. Fleischman, J. B. (1973).

MICHAEL =HOE E. EVIDENCE FOR RELATIONSHIP BETWEEN IDIOTYPIC DETERMINANTS AND HYPERVARIABLE REGIONS 1 . Structural Studies on Human Proteins with Shared ldiotypic Specificities a. Cold Agglutinins. Limited amino acid sequence analysis of ten human cold agglutinins by Capra et al. (1972) revealed that seven of the light chains belonged to the VKIII subgroup-a subgroup that comprises less than 40%of human kappa chains (Fig. 7 ) . Of these, three had identical sequences for thirty residues and three others differed by single substitutions.

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