Correspondence between structure and function of immunoglobulin G subclasses

V. P. Zav'yalov, V. M. Abramov, A. I. Ivannikov, O. I. Loseva, I. V. Dudich, E. I. Dudich, V. M. Tischenko, N. N. Khechinashvili, F. Franěk, G. Medgyesi, P. Závodszky, J. C. Jaton

Research output: Contribution to journalReview article

14 Citations (Scopus)

Abstract

The studies revealed essential differences in the internal flexibility within and between domains and in the energy of non-covalent interactions between domains and subunits of immunoglobulins of different subclasses and of different animals. The higher extent of non-covalent interactions between the Fab and Fc subunits correlates with the lower extent of interactions between the CH2 and CH3 domains (the higher flexibility of the FC parts). Hapten-binding induces conformational changes in the Fc subunits of the immunoglobulins with strong non-covalent interactions between the Fab and Fc subunits.

Original languageEnglish
Pages (from-to)85-94
Number of pages10
JournalHaematologia
Volume14
Issue number1
Publication statusPublished - Dec 1 1981

ASJC Scopus subject areas

  • Hematology

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  • Cite this

    Zav'yalov, V. P., Abramov, V. M., Ivannikov, A. I., Loseva, O. I., Dudich, I. V., Dudich, E. I., Tischenko, V. M., Khechinashvili, N. N., Franěk, F., Medgyesi, G., Závodszky, P., & Jaton, J. C. (1981). Correspondence between structure and function of immunoglobulin G subclasses. Haematologia, 14(1), 85-94.