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TitleAsymmetric binding of transferrin receptor to parvovirus capsids.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 104, Issue 16, Page 6585-6589, Year 2007
Publish dateApr 17, 2007
AuthorsSusan Hafenstein / Laura M Palermo / Victor A Kostyuchenko / Chuan Xiao / Marc C Morais / Christian D S Nelson / Valorie D Bowman / Anthony J Battisti / Paul R Chipman / Colin R Parrish / Michael G Rossmann /
PubMed AbstractAlthough many viruses are icosahedral when they initially bind to one or more receptor molecules on the cell surface, such an interaction is asymmetric, probably causing a breakdown in the symmetry ...Although many viruses are icosahedral when they initially bind to one or more receptor molecules on the cell surface, such an interaction is asymmetric, probably causing a breakdown in the symmetry and conformation of the original infecting virion in preparation for membrane penetration and release of the viral genome. Cryoelectron microscopy and biochemical analyses show that transferrin receptor, the cellular receptor for canine parvovirus, can bind to only one or a few of the 60 icosahedrally equivalent sites on the virion, indicating that either canine parvovirus has inherent asymmetry or binding of receptor induces asymmetry. The asymmetry of receptor binding to canine parvovirus is reminiscent of the special portal in tailed bacteriophages and some large, icosahedral viruses. Asymmetric interactions of icosahedral viruses with their hosts might be a more common phenomenon than previously thought and may have been obscured by averaging in previous crystallographic and electron microscopic structure determinations.
External linksProc Natl Acad Sci U S A / PubMed:17420467 / PubMed Central
MethodsEM (single particle)
Resolution27.0 Å
Structure data

EMDB-1287:
Asymmetric binding of transferrin receptor to parvovirus capsids.
Method: EM (single particle)

1288

2nsu

EMDB-1288: Asymmetric binding of transferrin receptor to parvovirus capsids.
PDB-2nsu: Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex
Method: EM (single particle) / Resolution: 27.0 Å

Source
  • Felis silvestris (wild cat)
  • homo sapiens (human)
KeywordsMETAL TRANSPORT / transferrin receptor / virus-receptor complex

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