We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ayn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ayn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ayn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ayn| PDB=1ayn | SCENE= }}
{{STRUCTURE_1ayn| PDB=1ayn | SCENE= }}
-
'''HUMAN RHINOVIRUS 16 COAT PROTEIN'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7915182}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7915182 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7915182}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Receptor]]
[[Category: Receptor]]
[[Category: Rhinovirus coat protein]]
[[Category: Rhinovirus coat protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:51:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:52:22 2008''

Revision as of 14:52, 30 June 2008

Image:1ayn.png

Template:STRUCTURE 1ayn

HUMAN RHINOVIRUS 16 COAT PROTEIN

Template:ABSTRACT PUBMED 7915182

About this Structure

1AYN is a Protein complex structure of sequences from Human rhinovirus sp.. This structure supersedes the now removed PDB entry 2rhn. 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

Page seeded by OCA on Mon Jun 30 17:52:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ayn"
Personal tools