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Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously.

X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein., Verdaguer N, Fita I, Reithmayer M, Moser R, Blaas D, Nat Struct Mol Biol. 2004 May;11(5):429-34. Epub 2004 Apr 4. PMID:15064754

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Homo sapiens | Human rhinovirus 2 | Blaas, D. | Fita, I. | Moser, R. | Reithmayer, M. | Verdaguer, N. | Human rhinovirus | Icosahedral virus | Virus-protein complex | Vldl-receptor