1ayn
From Proteopedia
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| - | [[Image:1ayn.gif|left|200px]]<br /> | + | [[Image:1ayn.gif|left|200px]]<br /><applet load="1ayn" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ayn" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ayn, resolution 2.9Å" /> | caption="1ayn, resolution 2.9Å" /> | ||
'''HUMAN RHINOVIRUS 16 COAT PROTEIN'''<br /> | '''HUMAN RHINOVIRUS 16 COAT PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AYN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_sp. Human rhinovirus sp.] with ZN, DAO and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2RHN. | + | 1AYN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_sp. Human rhinovirus sp.] with ZN, DAO and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2RHN. Known structural/functional Sites: <scene name='pdbsite=MYR:Myristylation Is Observed At N-Terminus Of Vp4, Which Li ...'>MYR</scene>, <scene name='pdbsite=POC:A Moiety Modelled As A 12-C Fatty Acid Is Observed In Fu ...'>POC</scene>, <scene name='pdbsite=RNA:RNA Observed Interacting w. These Residues On Interior S ...'>RNA</scene> and <scene name='pdbsite=ZN:Putative Zn Binding Site On Icosahedral Five-Fold Axis. ...'>ZN</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rhinovirus coat protein]] | [[Category: rhinovirus coat protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:23:33 2007'' |
Revision as of 12:13, 18 December 2007
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HUMAN RHINOVIRUS 16 COAT PROTEIN
Overview
BACKGROUND: Rhinoviruses and the homologous polioviruses have hydrophobic, pockets below their receptor-binding sites, which often contain, unidentified electron density ('pocket factors'). Certain antiviral, compounds also bind in the pocket, displacing the pocket factor and, inhibiting uncoating. However, human rhinovirus (HRV)14, which belongs to, the major group of rhinoviruses that use intercellular adhesion molecule-1, (ICAM-1) as a receptor, has an empty pocket. When antiviral compounds bind, into the empty pocket of HRV14, the roof of the pocket, which is also the, floor of the receptor binding site (the canyon), is deformed, preventing, receptor attachment. The role of the pocket in viral infectivity is not, known. RESULTS: We have determined the structure of HRV16, another major, receptor group rhinovirus serotype, to atomic resolution. Unlike HRV14, the pockets contain electron density resembling a fatty acid, eight or, more carbon atoms long. Binding of the antiviral compound WIN 56291 does, not cause deformation of the pocket, although it does prevent receptor, attachment. CONCLUSIONS: We conjecture that the binding of the receptor to, HRV16 can occur only when the pocket is temporarily empty, when it is, possible for the canyon floor to be deformed downwards into the pocket. We, further propose that the role of the pocket factor is to stabilize virus, in transit from one host cell to the next, and that binding of ICAM-1, traps the pocket in the empty state, destabilizing the virus as required, for uncoating.
About this Structure
1AYN is a Protein complex structure of sequences from Human rhinovirus sp. with ZN, DAO and MYR as ligands. This structure superseeds the now removed PDB entry 2RHN. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
The structure of human rhinovirus 16., Oliveira MA, Zhao R, Lee WM, Kremer MJ, Minor I, Rueckert RR, Diana GD, Pevear DC, Dutko FJ, McKinlay MA, et al., Structure. 1993 Sep 15;1(1):51-68. PMID:7915182
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