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PDBsum entry 3dpr
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Contents |
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269 a.a.
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250 a.a.
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237 a.a.
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25 a.a.
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39 a.a.
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References listed in PDB file
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Key reference
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Title
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Minor group human rhinovirus-Receptor interactions: geometry of multimodular attachment and basis of recognition.
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Authors
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J.Querol-Audí,
T.Konecsni,
J.Pous,
O.Carugo,
I.Fita,
N.Verdaguer,
D.Blaas.
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Ref.
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Febs Lett, 2009,
583,
235-240.
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PubMed id
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Abstract
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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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