1RVF

FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS

Summary for 1RVF

• Entry DOI: 10.2210/pdb1rvf/pdb
• Descriptor: HUMAN RHINOVIRUS 14 COAT PROTEIN, FAB 17-IA, ... (6 entities in total)
• Functional Keywords: polyprotein, coat protein, core protein, rna-directed rna polymerase, hydrolase, thiol protease, myristylation, complex (coat protein-immunoglobulin), icosahedral virus, virus-immune system complex, virus/immune system
• Biological source: Human rhinovirus 14; More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03303 P03303 P03303 P03303
• Total number of polymer chains: 6
• Total formula weight: 119373.17

Authors

Smith, T.J. (deposition date: 1996-09-05, release date: 1998-02-25, Last modification date: 2024-11-06)

Primary citation

Smith, T.J.,Chase, E.S.,Schmidt, T.J.,Olson, N.H.,Baker, T.S.
Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon.
Nature, 383:350-354, 1996

PubMed Abstract: The three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion has been determined to 4.0 angstrom resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody-antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds. Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system.

PubMed: 8848050
DOI: 10.1038/383350a0

Experimental method

X-RAY DIFFRACTION (4 Å)