1FOR

STRUCTURE DETERMINATION OF AN FAB FRAGMENT THAT NEUTRALIZES HUMAN RHINOVIRUS AND ANALYSIS OF THE FAB-VIRUS COMPLEX

Summary for 1FOR

• Entry DOI: 10.2210/pdb1for/pdb
• Descriptor: IGG2A-KAPPA 17-IA FAB (LIGHT CHAIN), IGG2A-KAPPA 17-IA FAB (HEAVY CHAIN) (3 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 46350.54

Authors

Smith, T.J.,Liu, H. (deposition date: 1994-05-24, release date: 1994-09-30, Last modification date: 2024-10-30)

Primary citation

Liu, H.,Smith, T.J.,Lee, W.M.,Mosser, A.G.,Rueckert, R.R.,Olson, N.H.,Cheng, R.H.,Baker, T.S.
Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab-virus complex.
J.Mol.Biol., 240:127-137, 1994

PubMed Abstract: The crystal structure of Fab17-IA, an antigen-binding fragment from a murine immunoglobulin that neutralizes human rhinovirus 14 (HRV14), has been solved to 2.7 A resolution. Fab17-IA crystallized into three different space groups depending upon the method used to purify the intact antibody. The structure was determined by use of molecular and isomorphous replacement methods. The current model has a crystallographic R-factor of approximately 19% for 10,192 independent reflections between 8 and 2.7 A. Correlation coefficient calculations showed that the Fab17-IA structure can be fit into the Fab17-IA/HRV14 image reconstruction density to within 5 A positional accuracy and to within a few degrees of rotation. The resulting interface of the docked antibody was examined and showed extensive charge and shape complementarity with the virus surface that was supported by site-directed mutagenesis experiments. The success of this approach validates the utility of combining X-ray crystallography with cryo-electron microscopy of complex macromolecular assemblies.

PubMed: 8027997
DOI: 10.1006/jmbi.1994.1427

Experimental method

X-RAY DIFFRACTION (2.75 Å)