Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872025 | FEBS Letters | 2009 | 6 Pages |
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.
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Authors
Jordi Querol-AudÃ, Tuende Konecsni, Joan Pous, Oliviero Carugo, Ignasi Fita, Nuria Verdaguer, Dieter Blaas,