2nsu | pdb_00002nsu
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Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex
Overview
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.
About this Structure
2NSU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Asymmetric binding of transferrin receptor to parvovirus capsids., Hafenstein S, Palermo LM, Kostyuchenko VA, Xiao C, Morais MC, Nelson CD, Bowman VD, Battisti AJ, Chipman PR, Parrish CR, Rossmann MG, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6585-9. Epub 2007 Apr 9. PMID:17420467
Page seeded by OCA on Mon Nov 12 23:02:26 2007
