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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 CSIC ORCID ; Fita, Ignacio CSIC ORCID ; Reithmayer, Manuela; Moser, Rosita; Blaas, Dieter | Fecha de publicación: | 4-abr-2004 | Editor: | Nature Publishing Group | Citación: | Nature Structural and Molecular Biology 11(5): 429-434 (2004) | Resumen: | 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. | Versión del editor: | http://dx.doi.org/10.1038/nsmb753 | URI: | http://hdl.handle.net/10261/110073 | DOI: | 10.1038/nsmb753 | Identificadores: | doi: 10.1038/nsmb753 issn: 1545-9993 |
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