Journal:PLoS ONE:1
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | [[Image:Polio.png|left|200px|thumb|Complete Poliovirus 2 Viron based on entry [[1eah]]]] | + | [[Image:Polio.png|left|200px|thumb|Complete Poliovirus 2 Viron based on PDB entry [[1eah]], example of 3-fold symmetry is in red, example of 5-fold symmetry is in blue ]] |
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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 three-fold and five-fold symmetry formed from 60 capsomeres containing one copy each | ||
| + | of viral capsid proteins VP1, VP2, VP3 and VP4 [1]. 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 | ||
| + | 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 12:59, 27 March 2011
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- ↑ DOI
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
