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The Structural Basis of Antibody Specificity

  • Conference paper
The Immune System

Part of the book series: Colloquium der Gesellschaft für Biologische Chemie ((MOSBACH,volume 27))

  • 199 Accesses

Abstract

The extraordinary capacity of the antibody-forming mechanism to make combining sites complementary to almost any molecular conformation of matter ranging in length from about 5Å to about 34Å (Kabat, 1976; Goodman, 1975) must ultimately be explained in structural, biosynthetic and genetic terms. While high resolution X-ray crystallography has now elucidated the structures of a number of combining sites including two Fab (Poljak et al., 1973; Segal et al., 1974), one light chain dimer (Schiffer et al., 1973) and an Fv fragment (Epp et al., 1974; see Davies and Padlan, 1976), it will manifestly be impossible to establish by this method the structures of a sufficiently large number of antibody combining sites of various specificities for us to map in detail the fitting of various antigenic determinants with their complementary regions in all antibody combining sites. Recent estimates suggest 107 clonotypes (Klinman et al., 1976) of antibody forming cells.

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Authors
  1. E. A. Kabat
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Editors and Affiliations

  1. Basel Institute of Immunology, 487 Grenzacherstraße, 4058, Basel, Switzerland

    Fritz Melchers

  2. Institut für Genetik, Weyertal 1, 5000, Köln, Germany

    Klaus Rajewsky

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Kabat, E.A. (1976). The Structural Basis of Antibody Specificity. In: Melchers, F., Rajewsky, K. (eds) The Immune System. Colloquium der Gesellschaft für Biologische Chemie, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81083-1_1

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  • DOI: https://doi.org/10.1007/978-3-642-81083-1_1

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-81085-5

  • Online ISBN: 978-3-642-81083-1

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