Aldo-keto reductase
From Proteopedia
(Difference between revisions)
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==Structural highlights == | ==Structural highlights == | ||
| - | The active site of AKR1B10 contains the cofactor <scene name='49/491879/Cv/ | + | The active site of AKR1B10 contains the cofactor <scene name='49/491879/Cv/8'>NADP</scene> and a <scene name='49/491879/Cv/9'>polyfluorinated inhibitor</scene>. Water molecules are shown as red spheres. |
| - | *<scene name='49/491879/Cv/ | + | *<scene name='49/491879/Cv/10'>Tyr and His </scene>are part of the enzyme catalytic tetrad<ref>PMID:24598757</ref>. |
| - | *<scene name='49/491879/Cv/ | + | *<scene name='49/491879/Cv/11'>NADP and polyfluorinated inhibitor are situated in the tunnel</scene>. |
</StructureSection> | </StructureSection> | ||
Revision as of 09:04, 3 January 2019
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3D structures of aldo-keto reductase
Updated on 03-January-2019
References
- ↑ Penning TM. The aldo-keto reductases (AKRs): Overview. Chem Biol Interact. 2015 Jun 5;234:236-46. doi: 10.1016/j.cbi.2014.09.024. Epub, 2014 Oct 7. PMID:25304492 doi:http://dx.doi.org/10.1016/j.cbi.2014.09.024
- ↑ Drury JE, Mindnich R, Penning TM. Characterization of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency. J Biol Chem. 2010 Aug 6;285(32):24529-37. doi: 10.1074/jbc.M110.127779. Epub 2010, Jun 3. PMID:20522910 doi:http://dx.doi.org/10.1074/jbc.M110.127779
- ↑ Cousido-Siah A, Ruiz FX, Mitschler A, Porte S, de Lera AR, Martin MJ, Manzanaro S, de la Fuente JA, Terwesten F, Betz M, Klebe G, Farres J, Pares X, Podjarny A. Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):889-903. doi:, 10.1107/S1399004713033452. Epub 2014 Feb 27. PMID:24598757 doi:http://dx.doi.org/10.1107/S1399004713033452
