4gqg

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'''Unreleased structure'''
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{{STRUCTURE_4gqg| PDB=4gqg | SCENE= }}
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===Crystal structure of AKR1B10 complexed with NADP+===
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The entry 4gqg is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/AK1BA_HUMAN AK1BA_HUMAN]] Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs.<ref>PMID:18087047</ref>
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Authors: Liping, Z., Xuehua, Z., Shangke, C., Jing, Z., Xiaopeng, H.
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==About this Structure==
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[[4gqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GQG OCA].
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Description: Crystal structure of AKR1B10 complexed with NADP+
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Jing, Z.]]
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[[Category: Liping, Z.]]
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[[Category: Shangke, C.]]
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[[Category: Xiaopeng, H.]]
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[[Category: Xuehua, Z.]]
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[[Category: Alpha-beta tim barrel]]
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[[Category: Nadp+]]
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[[Category: Nadp-dependant oxidoreductase]]
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[[Category: Oxidoreductase]]

Revision as of 07:36, 28 August 2013

Template:STRUCTURE 4gqg

Contents

Crystal structure of AKR1B10 complexed with NADP+

Function

[AK1BA_HUMAN] Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs.[1]

About this Structure

4gqg is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. Gallego O, Ruiz FX, Ardevol A, Dominguez M, Alvarez R, de Lera AR, Rovira C, Farres J, Fita I, Pares X. Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10. Proc Natl Acad Sci U S A. 2007 Dec 26;104(52):20764-9. Epub 2007 Dec 17. PMID:18087047

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