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X-Ray Diffraction Analysis of Immunoglobulin Structure

  • Conference paper
The Immune System

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

  • 201 Accesses

Abstract

The crystal structures of a human IgG antibody molecule Kol and a human Fc fragment have been determined at 4 Å and 3.5 Å resolution respectively by isomorphous replacement.

The electron-density maps were interpreted in terms of immunoglobulin domains based on the Rei and McPC 603 models (Kol) and by model-building (Fc).

The Kol Fab parts have a quarternary structure different from the fragments. The Fc part C-terminal to the hinge is disordered in the Kol crystals. There is no longitudinal V-C contact in Kol in contrast to Fab fragments. It is suggested that the Kol molecule is flexible in solution, while fragments are rigid.

In the Fc fragment both CH3 and CH2 show the immunoglobulin fold. The CH3 dimer aggregates as CH1 — CL while CH2 are widely separated from each other. The carbohydrate bound to Fc is in fixed position. From these structures it is suggested that antibody molecules are inherently flexible but become rigid upon interaction with antigen, which triggers the formation of all longitudinal contacts.

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Authors
  1. R. Huber
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  2. J. Deisenhofer
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  3. P. M. Colman
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  4. M. Matsushima
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  5. W. Palm
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Editor information

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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© 1976 Springer-Verlag Berlin · Heidelberg

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Huber, R., Deisenhofer, J., Colman, P.M., Matsushima, M., Palm, W. (1976). X-Ray Diffraction Analysis of Immunoglobulin Structure. 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_3

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  • DOI: https://doi.org/10.1007/978-3-642-81083-1_3

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-81085-5

  • Online ISBN: 978-3-642-81083-1

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