2alr

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{{STRUCTURE_2alr| PDB=2alr | SCENE= }}
{{STRUCTURE_2alr| PDB=2alr | SCENE= }}
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'''ALDEHYDE REDUCTASE'''
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===ALDEHYDE REDUCTASE===
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==Overview==
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The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.
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(as it appears on PubMed at http://www.pubmed.gov), where 15299353 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15299353}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:01:38 2008''

Revision as of 00:01, 29 July 2008

Image:2alr.png

Template:STRUCTURE 2alr

ALDEHYDE REDUCTASE

Template:ABSTRACT PUBMED 15299353

About this Structure

2ALR is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1alr. Full crystallographic information is available from OCA.

Reference

Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications., El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ, Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68. PMID:15299353

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