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.


1b9s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1b9s.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1b9s.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b9s| PDB=1b9s | SCENE= }}
{{STRUCTURE_1b9s| PDB=1b9s | SCENE= }}
-
'''NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN THE ACTIVE SITE'''
+
===NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN THE ACTIVE SITE===
-
==Overview==
+
<!--
-
The active site of type A or B influenza virus neuraminidase is composed of 11 conserved residues that directly interact with the substrate, sialic acid. An aromatic benzene ring has been used to replace the pyranose of sialic acid in our design of novel neuraminidase inhibitors. A bis(hydroxymethyl)pyrrolidinone ring was constructed in place of the N-acetyl group on the sialic acid. The hydroxymethyl groups replace two active site water molecules, which resulted in the high affinity of the nanomolar inhibitors. However, these inhibitors have greater potency for type A influenza virus than for type B influenza virus. To resolve the differences, we determined the X-ray crystal structure of three benzoic acid substituted inhibitors bound to the active site of B/Lee/40 neuraminidase. The investigation of a hydrophobic aliphatic group and a hydrophilic guanidino group on the aromatic inhibitors shows changes in the interaction with the active site residue Glu275. The results provide an explanation for the difference in efficacy of these inhibitors against types A and B viruses, even though the 11 active site residues of the neuraminidase are conserved.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10547289}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10547289 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10547289}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Neuraminidase]]
[[Category: Neuraminidase]]
[[Category: Sialidase]]
[[Category: Sialidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:15:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:39:18 2008''

Revision as of 15:39, 30 June 2008

Image:1b9s.png

Template:STRUCTURE 1b9s

NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN THE ACTIVE SITE

Template:ABSTRACT PUBMED 10547289

About this Structure

1B9S is a Single protein structure of sequence from Influenza b virus. Full crystallographic information is available from OCA.

Reference

Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site., Finley JB, Atigadda VR, Duarte F, Zhao JJ, Brouillette WJ, Air GM, Luo M, J Mol Biol. 1999 Nov 12;293(5):1107-19. PMID:10547289

Page seeded by OCA on Mon Jun 30 18:39:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b9s"
Personal tools