3fmg | pdb_00003fmg

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

spinqualitylabelsall models 3fmg, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fmg is a 3 chain structure with sequence from Mus musculus and Simian rotavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VP7_ROTRH Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In integrin-dependent strains, VP7 seems to essentially target the integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, once the initial attachment by VP4 has been achieved (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab.,Aoki ST, Settembre EC, Trask SD, Greenberg HB, Harrison SC, Dormitzer PR Science. 2009 Jun 12;324(5933):1444-7. PMID:19520960 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody 3D structures Monoclonal Antibodies 3D structures 3D structures of non-human antibody

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