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.


2agt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2agt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2agt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2agt| PDB=2agt | SCENE= }}
{{STRUCTURE_2agt| PDB=2agt | SCENE= }}
-
'''Aldose Reductase Mutant Leu 300 Pro complexed with Fidarestat'''
+
===Aldose Reductase Mutant Leu 300 Pro complexed with Fidarestat===
-
==Overview==
+
<!--
-
Structure of the Leu300Pro mutant of human aldose reductase (ALR2) in complex with the inhibitor fidarestat is determined. Comparison with the hALR2-fidarestat complex and the porcine aldehyde reductase (ALR1)-fidarestat complex indicates that the hydrogen bond between the Leu300 amino group of the wild-type and the exocyclic amide group of the inhibitor is the key determinant for the specificity of fidarestat for ALR2 over ALR1. Thermodynamic data also suggest an enthalpic contribution as the predominant difference in the binding energy between the aldose reductase mutant and the wild-type. An additional selectivity-determining feature is the difference in the interaction between the inhibitor and the side chain of Trp219, ordered in the present structure but disordered (corresponding Trp220) in the ALR1-fidarestat complex. Thus, the hydrogen bond ( approximately 7 kJ/mol) corresponds to a 23-fold difference in inhibitor potency while the differences in the interactions between Trp219(ALR2) and fidarestat and between Trp220(ALR1) and fidarestat can account for an additional 10-fold difference in potency.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16134934}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16134934 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16134934}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Nadp]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:01:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:17:35 2008''

Revision as of 14:17, 28 July 2008

Image:2agt.png

Template:STRUCTURE 2agt

Aldose Reductase Mutant Leu 300 Pro complexed with Fidarestat

Template:ABSTRACT PUBMED 16134934

About this Structure

2AGT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Factorizing selectivity determinants of inhibitor binding toward aldose and aldehyde reductases: structural and thermodynamic properties of the aldose reductase mutant Leu300Pro-fidarestat complex., Petrova T, Steuber H, Hazemann I, Cousido-Siah A, Mitschler A, Chung R, Oka M, Klebe G, El-Kabbani O, Joachimiak A, Podjarny A, J Med Chem. 2005 Sep 8;48(18):5659-65. PMID:16134934

Page seeded by OCA on Mon Jul 28 17:17:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2agt"
Personal tools