Journal:PLoS ONE:1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
[[Image:Polio.png|left|200px|thumb|Complete Poliovirus 2 Viron based on PDB entry [[1eah]], <font color='red'><b>example of 3-fold symmetry is in red</b></font>, <font color='blue'><b>example of 5-fold symmetry is in blue</b></font> ]]
[[Image:Polio.png|left|200px|thumb|Complete Poliovirus 2 Viron based on PDB entry [[1eah]], <font color='red'><b>example of 3-fold symmetry is in red</b></font>, <font color='blue'><b>example of 5-fold symmetry is in blue</b></font> ]]
-
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 <scene name='Journal:PLoS_ONE:1/F1/3'>capsomeres containing one copy</scene> each of viral capsid proteins VP1 (light blue), VP2 (pale green), VP3 (light orange) and VP4(light magenta). 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
-
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
+
palmitic and myristic acids and hydrophobic compounds, that stabilize the capsid and whose removal is a necessary prerequisite for uncoating.
palmitic and myristic acids and hydrophobic compounds, that stabilize the capsid and whose removal is a necessary prerequisite for uncoating.

Revision as of 15:01, 27 March 2011

Drag the structure with the mouse to rotate
  1. DOI

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky

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.
Personal tools