title: X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.
abstract: 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.
authors.affiliation: Institut de Biologia Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Jordi Girona 18-26, E-08034 Barcelona, Spain. nvmcri@ibmb.csis.es
authors.forename: Nuria
authors.initials: N
authors.lastname: Verdaguer
authors.forename: Ignacio
authors.initials: I
authors.lastname: Fita
authors.forename: Manuela
authors.initials: M
authors.lastname: Reithmayer
authors.forename: Rosita
authors.initials: R
authors.lastname: Moser
authors.forename: Dieter
authors.initials: D
authors.lastname: Blaas
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011485:Protein Binding; D011991:Receptors, Virus / Q000378:metabolism*; D012229:Rhinovirus / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D011991:Receptors, Virus