1rhi
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1rhi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rhi, resolution 3.0Å" /> '''HUMAN RHINOVIRUS 3 CO...)
Next diff →
Revision as of 23:28, 20 November 2007
|
HUMAN RHINOVIRUS 3 COAT PROTEIN
Overview
BACKGROUND: The over 100 serotypes of human rhinoviruses (HRV) are major, causative agents of the common cold in humans. These HRVs can be roughly, divided into a major and minor group according to their cellular, receptors. They can also be divided into two antiviral groups, A and B, based on their sensitivity to different capsid-binding antiviral, compounds. The crystal structures of HRV14 and HRV16, major-receptor group, rhinoviruses, as well as HRV1A, a minor-receptor group rhinovirus, were, determined previously. Sequence comparisons had shown that HRV14 seemed to, be an outlier among rhinoviruses. Furthermore, HRV14 was the only virus, with no cellular 'pocket factor' in a hydrophobic pocket which is targeted, by many capsid-binding antiviral compounds and is thought to regulate, viral stability. HRV3, another major-receptor group virus, was chosen for, study because it is one of a subset of serotypes that best represents the, drug sensitivity of most rhinovirus serotypes. Both HRV3 and HRV14 belong, to antiviral group A, while HRV16 and HRV1A belong to antiviral group B., RESULTS: HRV3 was found to be very similar to HRV14 in sequence and, structure. Like HRV14, crystallized HRV3 also has no bound pocket factor., The structure of HRV3 complexed with an antiviral compound, WIN56291, was, also determined and found to be similar to the same antiviral compound, complexed with HRV14. CONCLUSIONS: The amino-acid sequence and structural, similarity between HRV3 and HRV14 suggests that rhinoviruses in the same, antiviral group have similar amino-acid sequences and structures. The, similar amino-acid composition in the pocket region and the viral protein, VP1 N termini in all known group B HRV sequences suggests that these, viruses may all contain pocket factors and ordered N-terminal amphipathic, helices in VP1. Both of these factors contribute to viral stability, which, is consistent with the observations that group B rhinoviruses have a, higher chance of successful transmission from one host to another and is a, possible explanation for the observed higher pathogenicity of these, rhinoviruses.
About this Structure
1RHI is a Protein complex structure of sequences from Human rhinovirus 2 with CA as ligand. Full crystallographic information is available from OCA.
Reference
Human rhinovirus 3 at 3.0 A resolution., Zhao R, Pevear DC, Kremer MJ, Giranda VL, Kofron JA, Kuhn RJ, Rossmann MG, Structure. 1996 Oct 15;4(10):1205-20. PMID:8939746
Page seeded by OCA on Wed Nov 21 01:36:13 2007
