title: Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition.
abstract: X-ray structures of human rhinovirus 2 (HRV2) in complex with soluble very-low-density lipoprotein receptors encompassing modules 1, 2, and 3 (V123) and five V3 modules arranged in tandem (V33333) demonstrates multi-modular binding around the virion's five-fold axes. Occupancy was 60% for V123 and 100% for V33333 explaining the high-avidity of the interaction. Surface potentials of 3D-models of all minor group HRVs and K-type major group HRVs were compared; hydrophobic interactions between a conserved lysine in the viruses and a tryptophan in the receptor modules together with coulombic attraction via diffuse opposite surface potentials determine minor group HRV receptor specificity.
authors.affiliation: Institut de Biologia Molecular de Barcelona (CSIC), Parc Científic de Barcelona, Barcelona, Spain.
authors.forename: Jordi
authors.initials: J
authors.lastname: Querol-Audí
authors.forename: Tuende
authors.initials: T
authors.lastname: Konecsni
authors.forename: Joan
authors.initials: J
authors.lastname: Pous
authors.forename: Oliviero
authors.initials: O
authors.lastname: Carugo
authors.forename: Ignasi
authors.initials: I
authors.lastname: Fita
authors.forename: Nuria
authors.initials: N
authors.lastname: Verdaguer
authors.forename: Dieter
authors.initials: D
authors.lastname: Blaas
mesh_terms: D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011973:Receptors, LDL / Q000737:chemistry* / Q000502:physiology; D011991:Receptors, Virus / Q000737:chemistry* / Q000502:physiology; D012229:Rhinovirus / Q000737:chemistry* / Q000502:physiology
chemical_list: D011973:Receptors, LDL; D011991:Receptors, Virus; C036053:VLDL receptor