4gqg

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	{{STRUCTURE_4gqg| PDB=4gqg | SCENE= }}		{{STRUCTURE_4gqg| PDB=4gqg | SCENE= }}
	===Crystal structure of AKR1B10 complexed with NADP+===		===Crystal structure of AKR1B10 complexed with NADP+===
		+	{{ABSTRACT_PUBMED_24100137}}
	==Function==		==Function==
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	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024100137</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Jing, Z.]]	+	[[Category: Chen, S.]]
-	[[Category: Liping, Z.]]	+	[[Category: Hu, X.]]
-	[[Category: Shangke, C.]]	+	[[Category: Zhai, J.]]
-	[[Category: Xiaopeng, H.]]	+	[[Category: Zhang, L.]]
-	[[Category: Xuehua, Z.]]	+	[[Category: Zheng, X.]]
	[[Category: Alpha-beta tim barrel]]		[[Category: Alpha-beta tim barrel]]
	[[Category: Nadp+]]		[[Category: Nadp+]]
	[[Category: Nadp-dependant oxidoreductase]]		[[Category: Nadp-dependant oxidoreductase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

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Revision as of 05:18, 23 October 2013

Template:STRUCTURE 4gqg

Contents 1 Crystal structure of AKR1B10 complexed with NADP+ 2 Function 3 About this Structure 4 Reference

Crystal structure of AKR1B10 complexed with NADP+

Template:ABSTRACT PUBMED 24100137

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

• Zhang L, Zhang H, Zhao Y, Li Z, Chen S, Zhai J, Chen Y, Xie W, Wang Z, Li Q, Zheng X, Hu X. Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111). FEBS Lett. 2013 Oct 4. pii: S0014-5793(13)00726-6. doi:, 10.1016/j.febslet.2013.09.031. PMID:24100137 doi:http://dx.doi.org/10.1016/j.febslet.2013.09.031

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