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Título

X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein

Autor Verdaguer, Núria ; Fita, Ignacio ; Reithmayer, Manuela; Moser, Rosita; Blaas, Dieter
Fecha de publicación 4-abr-2004
EditorNature Publishing Group
Citación Nature Structural and Molecular Biology 11(5): 429-434 (2004)
ResumenAlthough 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.
Versión del editorhttp://dx.doi.org/10.1038/nsmb753
URI http://hdl.handle.net/10261/110073
DOI10.1038/nsmb753
Identificadoresdoi: 10.1038/nsmb753
issn: 1545-9993
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