1BBD

THREE DIMENSIONAL STRUCTURE OF THE FAB FRAGMENT OF A NEUTRALIZING ANTIBODY TO HUMAN RHINOVIRUS SEROTYPE 2

Summary for 1BBD

• Entry DOI: 10.2210/pdb1bbd/pdb
• Descriptor: IGG2A-KAPPA 8F5 FAB (LIGHT CHAIN), IGG2A-KAPPA 8F5 FAB (HEAVY CHAIN), SULFATE ION, ... (4 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 48101.25

Authors

Tormo, J.,Blaas, D.,Fita, I. (deposition date: 1992-05-05, release date: 1994-01-31, Last modification date: 2024-10-23)

Primary citation

Tormo, J.,Stadler, E.,Skern, T.,Auer, H.,Kanzler, O.,Betzel, C.,Blaas, D.,Fita, I.
Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2.
Protein Sci., 1:1154-1161, 1992

PubMed Abstract: The crystal structure of the antigen-binding fragment of a monoclonal antibody (8F5) that neutralizes human rhinovirus serotype 2 has been determined by X-ray diffraction studies. Antibody 8F5, obtained by immunization with native HRV2 virions, cross-reacts with peptides of the viral capsid protein VP2, which contribute to the neutralizing immunogenic site B in this serotype. The structure was solved by the molecular replacement method and has been refined to an R-factor of 18.9% at 2.8 A resolution. The elbow angle, relating the variable and constant modules of the molecule is 127 degrees, representing the smallest elbow angle observed so far in an Fab fragment. Furthermore, the charged residues of the epitope can be well accommodated in the antigen-binding site. This is the first crystal structure reported for an antibody directed against an icosahedral virus.

PubMed: 1338980

Experimental method

X-RAY DIFFRACTION (2.8 Å)