2alr
From Proteopedia
(New page: 200px<br /> <applet load="2alr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2alr, resolution 2.48Å" /> '''ALDEHYDE REDUCTASE'...) |
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| - | [[Image:2alr.gif|left|200px]]<br /> | + | [[Image:2alr.gif|left|200px]]<br /><applet load="2alr" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2alr" size=" | + | |
caption="2alr, resolution 2.48Å" /> | caption="2alr, resolution 2.48Å" /> | ||
'''ALDEHYDE REDUCTASE'''<br /> | '''ALDEHYDE REDUCTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of porcine and human aldehyde reductase, an enzyme | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ALR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure | + | 2ALR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1ALR. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:36 2008'' |
Revision as of 14:28, 21 February 2008
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ALDEHYDE REDUCTASE
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Allergic rhinitis, susceptibility to OMIM:[147683], Asthma, susceptibility to OMIM:[147683]
About this Structure
2ALR is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1ALR. Active as Alcohol dehydrogenase (NADP(+)), with EC number 1.1.1.2 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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