Antibody--hapten interactions in solution

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
R A DwekA I White

Abstract

This paper reports the initial progress in a research programme to identify and obtain the relative orientations, in solution, of the amino acid residues that constitute the combining site of the myeloma protein MOPC 315. This protein has a molecular mass of 150,000, but enzymic digestion yields the Fv fragment of molecular mass 25,000 which still has the combining site intact, as judged by the affinity for dinitrophenyl haptens. Analysis of the e.s.r. spectra of a series of dinitrophenyl spin labelled haptens has allowed the dimensions, rigidity and polarity profile of the combining site to be determined. The combining site is a cleft of overall dimensions 1.1 nm x 0.9 nm x 0.6 nm which has considerable structural rigidity. One of these spin labels has also been used to perturb the n.m.r. spectrum of the Fv and using difference spectroscopy the 270 MHz proton n.m.r. spectrum of the amino acid residues in and around the combining site has been obtained. This spectrum contains only the equivalent of about 30 aromatic and 21 aliphatic protons. Comparison of this difference spectrum with that obtained using a diamagnetic analogue suggests that any conformational changes on hapten binding are mainly localized to the combining site....Continue Reading

Citations

Mar 1, 1981·Molecular Immunology·Y H JouD Pressman
Oct 13, 2006·Annual Review of Immunology·James N ArnoldR A Dwek
Dec 1, 1976·European Journal of Biochemistry·D MarshG A Ritchie

Related Concepts

Antigen-Antibody Reactions
Binding Sites, Antibody
Electron Spin Resonance Spectroscopy
Gadolinium
Haptens
Histidine
Hydrogen-Ion Concentration
IgA2
Fab Immunoglobulins
Lanthanum

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