Structural highlights
Function
IGKC_MOUSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody.,Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A. Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652
