1FAI

THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY

Summary for 1FAI

• Entry DOI: 10.2210/pdb1fai/pdb
• Related: 2F19
• Descriptor: IGG2B-KAPPA R19.9 FAB (LIGHT CHAIN), IGG2B-KAPPA R19.9 FAB (HEAVY CHAIN) (2 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 47256.36

Authors

Lascombe, M.B.,Alzari, P.M.,Poljak, R.J.,Nisonoff, A. (deposition date: 1992-05-27, release date: 1992-10-15, Last modification date: 2024-11-20)

Primary citation

Lascombe, M.B.,Alzari, P.M.,Poljak, R.J.,Nisonoff, A.
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody.
Proc.Natl.Acad.Sci.USA, 89:9429-9433, 1992

PubMed 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.

PubMed: 1409652
DOI: 10.1073/pnas.89.20.9429

Experimental method

X-RAY DIFFRACTION (2.7 Å)