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. 1992 Oct 15;89(20):9429–9433. doi: 10.1073/pnas.89.20.9429

Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody.

M B Lascombe 1, P M Alzari 1, R J Poljak 1, A Nisonoff 1
PMCID: PMC50145  PMID: 1409652

Abstract

The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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