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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Proceedings of the National Academy of Sciences of the United States of America

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 15 Oct 1992

Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A

Link to Pubmed [PMID] – 1409652

Proc. Natl. Acad. Sci. U.S.A. 1992 Oct;89(20):9429-33

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.

http://www.ncbi.nlm.nih.gov/pubmed/1409652