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.

2ao0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ao0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ao0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ao0| PDB=2ao0 | SCENE= }}
{{STRUCTURE_2ao0| PDB=2ao0 | SCENE= }}
-
'''Structure of Aldehyde Reductase Holoenzyme in Complex with the Potent Aldose Reductase Inhibitor Fidarestat: Implications for Inhibitor Binding and Selectivity'''
+
===Structure of Aldehyde Reductase Holoenzyme in Complex with the Potent Aldose Reductase Inhibitor Fidarestat: Implications for Inhibitor Binding and Selectivity===
-
==Overview==
+
<!--
-
Structure determination of porcine aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat was carried out to explain the difference in the potency of the inhibitor for aldose and aldehyde reductases. The hydrogen bonds between the active-site residues Tyr50, His113, and Trp114 and fidarestat are conserved in the two enzymes. In aldose reductase, Leu300 forms a hydrogen bond through its main-chain nitrogen atom with the exocyclic amide group of the inhibitor, which when replaced with a Pro in aldehyde reductase, cannot form a hydrogen bond, thus causing a loss in binding energy. Furthermore, in aldehyde reductase, the side chain of Trp220 occupies a disordered split conformation that is not observed in aldose reductase. Molecular modeling and inhibitory activity measurements suggest that the difference in the interaction between the side chain of Trp220 and fidarestat may contribute to the difference in the binding of the inhibitor to the enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16107153}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16107153 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16107153}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Ternary complex]]
[[Category: Ternary complex]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:16:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:58:13 2008''

Revision as of 01:58, 28 July 2008

Template:STRUCTURE 2ao0

Structure of Aldehyde Reductase Holoenzyme in Complex with the Potent Aldose Reductase Inhibitor Fidarestat: Implications for Inhibitor Binding and Selectivity

Template:ABSTRACT PUBMED 16107153

About this Structure

2AO0 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity., El-Kabbani O, Carbone V, Darmanin C, Oka M, Mitschler A, Podjarny A, Schulze-Briese C, Chung RP, J Med Chem. 2005 Aug 25;48(17):5536-42. PMID:16107153

Page seeded by OCA on Mon Jul 28 04:58:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools