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.

1qjx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qjx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qjx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qjx| PDB=1qjx | SCENE= }}
{{STRUCTURE_1qjx| PDB=1qjx | SCENE= }}
-
'''HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934'''
+
===HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934===
-
==Overview==
+
<!--
-
Rhinoviruses are a frequent cause of the common cold. A series of antirhinoviral compounds have been developed that bind into a hydrophobic pocket in the viral capsid, stabilizing the capsid and interfering with cell attachment. The structures of a variety of such compounds, complexed with rhinovirus serotypes 14, 16, 1A, and 3, previously have been examined. Three chemically similar compounds, closely related to a drug that is undergoing phase III clinical trials, were chosen to determine the structural impact of the heteroatoms in one of the three rings. The compounds were found to have binding modes that depend on their electronic distribution. In the compound with the lowest efficacy, the terminal ring is displaced by 1 A and rotated by 180 degrees relative to the structure of the other two. The greater polarity of the terminal ring in one of the three compounds leads to a small displacement of its position relative to the other compounds in the hydrophobic end of the antiviral compound binding pocket to a site where it makes fewer interactions. Its lower efficacy is likely to be the result of the reduced number of interactions. A region of conserved residues has been identified near the entrance to the binding pocket where there is a corresponding conservation of the mode of binding of these compounds to different serotypes. Thus, variations in residues lining the more hydrophobic end of the pocket are primarily responsible for the differences in drug efficacies.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10611281}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10611281 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10611281}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Rhinovirus coat protein]]
[[Category: Rhinovirus coat protein]]
[[Category: Win compound]]
[[Category: Win compound]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:21:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:10:30 2008''

Revision as of 20:10, 28 July 2008

Image:1qjx.png

Template:STRUCTURE 1qjx

HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934

Template:ABSTRACT PUBMED 10611281

About this Structure

1QJX is a Protein complex structure of sequences from Human rhinovirus 16. Full crystallographic information is available from OCA.

Reference

Analysis of three structurally related antiviral compounds in complex with human rhinovirus 16., Hadfield AT, Diana GD, Rossmann MG, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14730-5. PMID:10611281

Page seeded by OCA on Mon Jul 28 23:10:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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