This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1vcj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vcj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vcj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vcj| PDB=1vcj | SCENE= }}
{{STRUCTURE_1vcj| PDB=1vcj | SCENE= }}
-
'''Influenza B virus neuraminidase complexed with 1-(4-Carboxy-2-(3-pentylamino)phenyl)-5-aminomethyl-5-hydroxymethyl-pyrrolidin-2-one'''
+
===Influenza B virus neuraminidase complexed with 1-(4-Carboxy-2-(3-pentylamino)phenyl)-5-aminomethyl-5-hydroxymethyl-pyrrolidin-2-one===
-
==Overview==
+
<!--
-
Owing to the highly conserved nature of its active site, Influenza B virus neuraminidase (NA) has emerged as a major target for the design of novel anti-influenza drugs. A benzene-ring scaffold has been used in place of the pyranose ring of sialic acid to develop simpler NA inhibitors that contain a minimal number of chiral centers. A new compound belonging to this series, BANA 207, showed significant improvement in inhibitory activity against Influenza B virus NA compared with its parent compound. Here, the structural analysis of a complex of BANA 207 with influenza virus B/Lee/40 NA is reported. The results indicate that BANA 207 forms an unexpected interaction with the crucial active-site residue Glu275 that stabilizes the side chain of this residue in a conformation previously unobserved in NA-inhibitor complexes. This change in the side-chain orientation of Glu275 alters the topology of the triglycerol pocket, which accommodates an additional lipophilic substitution at the benzene ring and may provide an explanation for the increased activity of BANA 207 against Influenza B virus NA.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15159560}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15159560 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15159560}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Protein-inhibitor complex]]
[[Category: Protein-inhibitor complex]]
[[Category: Small molecule inhibitor]]
[[Category: Small molecule inhibitor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:22:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:18:44 2008''

Revision as of 23:18, 28 July 2008

Image:1vcj.png

Template:STRUCTURE 1vcj

Influenza B virus neuraminidase complexed with 1-(4-Carboxy-2-(3-pentylamino)phenyl)-5-aminomethyl-5-hydroxymethyl-pyrrolidin-2-one

Template:ABSTRACT PUBMED 15159560

About this Structure

1VCJ is a Single protein structure of sequence from Influenza b virus. This structure supersedes the now removed PDB entry 1uja. Full crystallographic information is available from OCA.

Reference

A benzoic acid inhibitor induces a novel conformational change in the active site of Influenza B virus neuraminidase., Lommer BS, Ali SM, Bajpai SN, Brouillette WJ, Air GM, Luo M, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1017-23. Epub 2004, May 21. PMID:15159560

Page seeded by OCA on Tue Jul 29 02:18:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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