X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.
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.
Verdaguer
Nuria
N
Institut de Biologia Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Jordi Girona 18-26, E-08034 Barcelona, Spain. nvmcri@ibmb.csis.es
Fita
Ignacio
I
Reithmayer
Manuela
M
Moser
Rosita
R
Blaas
Dieter
D
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
D011991:Receptors, Virus