1a4g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a4g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a4g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a4g| PDB=1a4g | SCENE= }}
{{STRUCTURE_1a4g| PDB=1a4g | SCENE= }}
-
'''INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH ZANAMIVIR'''
+
===INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH ZANAMIVIR===
-
==Overview==
+
<!--
-
The first paper in this series (see previous article) described structure-activity studies of carboxamide analogues of zanamivir binding to influenza virus sialidase types A and B and showed that inhibitory activity of these compounds was much greater against influenza A enzyme. To understand the large differences in affinities, a number of protein-ligand complexes have been investigated using crystallography and molecular dynamics. The crystallographic studies show that the binding of ligands containing tertiary amide groups is accompanied by the formation of an intramolecular planar salt bridge between two amino acid residues in the active site of the enzyme. It is proposed that the unexpected strong binding of these inhibitors is a result of the burial of hydrophobic surface area and salt-bridge formation in an environment of low dielectric. In sialidase from type A virus, binding of the carboxamide moeity and salt-bridge formation have only a minor effect on the positions of the surrounding residues, whereas in type B enzyme, significant distortion of the protein is observed. The results suggest that the decreased affinity in enzyme from influenza B is directly correlated with the small changes that occur in the amino acid residue interactions accompanying ligand binding. Molecular dynamics calculations have shown that the tendency for salt-bridge formation is greater in influenza A sialidase than influenza B sialidase and that this tendency is a useful descriptor for the prediction of inhibitor potency.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9526556}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9526556 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9526556}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Glycosylated protein]]
[[Category: Glycosylated protein]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:47:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:05:58 2008''

Revision as of 13:06, 30 June 2008

Image:1a4g.png

Template:STRUCTURE 1a4g

INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH ZANAMIVIR

Template:ABSTRACT PUBMED 9526556

About this Structure

1A4G is a Single protein structure of sequence from Influenza b virus. Full crystallographic information is available from OCA.

Reference

Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B., Taylor NR, Cleasby A, Singh O, Skarzynski T, Wonacott AJ, Smith PW, Sollis SL, Howes PD, Cherry PC, Bethell R, Colman P, Varghese J, J Med Chem. 1998 Mar 12;41(6):798-807. PMID:9526556

Page seeded by OCA on Mon Jun 30 16:05:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a4g"
Personal tools