Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FMG

Structure of rotavirus outer capsid protein VP7 trimer in complex with a neutralizing Fab

Summary for 3FMG
Entry DOI10.2210/pdb3fmg/pdb
DescriptorFab of neutralizing antibody 4F8, light chain, Fab of neutralizing antibody 4F8, heavy chain, Glycoprotein VP7, ... (4 entities in total)
Functional Keywordsantibody-antigen complex, calcium dependent trimer, antiparallel beta-sandwich, jelly roll, alpha-beta-alpha sandwich, rossmann fold, capsid protein, endoplasmic reticulum, glycoprotein, membrane, transmembrane, virion, immune system
Biological sourceSimian rotavirus
More
Cellular locationVirion (By similarity): P12476
Total number of polymer chains3
Total formula weight78281.81
Authors
Aoki, S.T.,Settembre, E.C.,Trask, S.D.,Greenberg, H.B.,Harrison, S.C.,Dormitzer, P.R. (deposition date: 2008-12-22, release date: 2009-06-23, Last modification date: 2024-11-27)
Primary citationAoki, S.T.,Settembre, E.C.,Trask, S.D.,Greenberg, H.B.,Harrison, S.C.,Dormitzer, P.R.
Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab.
Science, 324:1444-1447, 2009
Cited by
PubMed Abstract: Rotavirus outer-layer protein VP7 is a principal target of protective antibodies. Removal of free calcium ions (Ca2+) dissociates VP7 trimers into monomers, releasing VP7 from the virion, and initiates penetration-inducing conformational changes in the other outer-layer protein, VP4. We report the crystal structure at 3.4 angstrom resolution of VP7 bound with the Fab fragment of a neutralizing monoclonal antibody. The Fab binds across the outer surface of the intersubunit contact, which contains two Ca2+ sites. Mutations that escape neutralization by other antibodies suggest that the same region bears the epitopes of most neutralizing antibodies. The monovalent Fab is sufficient to neutralize infectivity. We propose that neutralizing antibodies against VP7 act by stabilizing the trimer, thereby inhibiting the uncoating trigger for VP4 rearrangement. A disulfide-linked trimer is a potential subunit immunogen.
PubMed: 19520960
DOI: 10.1126/science.1170481
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon