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Journal:PLoS ONE:1
From Proteopedia
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Poliovirus is a member of the ''Picornaviridae''. Like other members of the ''Picornaviridae'', poliovirus RNA is encapsulated in an icosahedral structure with axes of <scene name='Journal:PLoS_ONE:1/F43/1'>three-fold</scene> and <scene name='Journal:PLoS_ONE:1/F45/1'>five-fold</scene> symmetry formed from 60 capsomeres containing one copy each | Poliovirus is a member of the ''Picornaviridae''. Like other members of the ''Picornaviridae'', poliovirus RNA is encapsulated in an icosahedral structure with axes of <scene name='Journal:PLoS_ONE:1/F43/1'>three-fold</scene> and <scene name='Journal:PLoS_ONE:1/F45/1'>five-fold</scene> symmetry formed from 60 capsomeres containing one copy each | ||
| - | of viral capsid proteins VP1, VP2, VP3 and VP4 | + | of viral capsid proteins VP1, VP2, VP3 and VP4. The binding site for the human poliovirus receptor is located in a canyon at the five-fold axis of symmetry. The VP1 of picornaviruses contain a hydrophobic pocket that is accessed through this canyon. This pocket is normally occupied by pocket factors, sphingosine-like molecules including |
| - | poliovirus receptor is located in a canyon at the five-fold axis of symmetry. The VP1 of | + | palmitic and myristic acids and hydrophobic compounds, that stabilize the capsid and whose removal is a necessary prerequisite for uncoating. |
| - | picornaviruses contain a hydrophobic pocket that is accessed through this canyon. This | + | |
| - | pocket is normally occupied by pocket factors, sphingosine-like molecules including | + | |
| - | palmitic and myristic acids and hydrophobic compounds, that stabilize the capsid and | + | |
| - | whose removal is a necessary prerequisite for uncoating | + | |
<scene name='Journal:PLoS_ONE:1/F41/2'>TextToBeDisplayed</scene> | <scene name='Journal:PLoS_ONE:1/F41/2'>TextToBeDisplayed</scene> | ||
Revision as of 14:23, 27 March 2011
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- ↑ DOI
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