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4i5x
From Proteopedia
(Difference between revisions)
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| - | + | {{STRUCTURE_4i5x| PDB=4i5x | SCENE= }} | |
| + | ===Crystal Structure Of AKR1B10 Complexed With NADP+ And Flufenamic acid=== | ||
| + | {{ABSTRACT_PUBMED_24100137}} | ||
| - | + | ==Function== | |
| + | [[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> | ||
| - | + | ==About this Structure== | |
| + | [[4i5x]] 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=4I5X OCA]. | ||
| - | + | ==Reference== | |
| + | <ref group="xtra">PMID:024100137</ref><references group="xtra"/><references/> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Chen, S.]] | ||
| + | [[Category: Zhai, J.]] | ||
| + | [[Category: Zhang, H.]] | ||
| + | [[Category: Zhang, L.]] | ||
| + | [[Category: Zhao, Y.]] | ||
| + | [[Category: Zheng, X.]] | ||
| + | [[Category: Aldo-keto reductase]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Tim barrel]] | ||
Revision as of 06:43, 23 October 2013
Contents |
Crystal Structure Of AKR1B10 Complexed With NADP+ And Flufenamic acid
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
4i5x 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
- ↑ 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
Categories: Homo sapiens | Chen, S. | Zhai, J. | Zhang, H. | Zhang, L. | Zhao, Y. | Zheng, X. | Aldo-keto reductase | Oxidoreductase | Tim barrel
