Aldo-keto reductase
From Proteopedia
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*<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/10'>Tyr and His </scene>are part of the enzyme catalytic tetrad<ref>PMID:24598757</ref>. | ||
*<scene name='49/491879/Cv/11'>NADP and polyfluorinated inhibitor are situated in the tunnel</scene>. | *<scene name='49/491879/Cv/11'>NADP and polyfluorinated inhibitor are situated in the tunnel</scene>. | ||
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| + | ==3D structures of aldo-keto reductase== | ||
| + | [[Aldo-keto reductase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[4xzm]], [[4gqg]] – hAKR1B10 + NADP <br /> | **[[4xzm]], [[4gqg]] – hAKR1B10 + NADP <br /> | ||
**[[4xzn]] – hAKR1B10 (mutant) + NADP <br /> | **[[4xzn]] – hAKR1B10 (mutant) + NADP <br /> | ||
| - | **[[4jih]], [[4jii]], [[4i5x]] – hAKR1B10 + NADP + inhibitor <br /> | + | **[[4jih]], [[4jii]], [[4i5x]], [[5y7n]] – hAKR1B10 + NADP + inhibitor <br /> |
**[[4ga8]], [[4gab]], [[1zua]], [[5liy]], [[5lik]], [[5liu]], [[5liw]], [[5lix]], [[4xzl]], [[4wev]], [[4icc]], [[5m2f]] – hAKR1B10 (mutant) + NADP + inhibitor <br /> | **[[4ga8]], [[4gab]], [[1zua]], [[5liy]], [[5lik]], [[5liu]], [[5liw]], [[5lix]], [[4xzl]], [[4wev]], [[4icc]], [[5m2f]] – hAKR1B10 (mutant) + NADP + inhibitor <br /> | ||
**[[4gq0]] – hAKR1B10 + NADP + caffeic acid ester<br /> | **[[4gq0]] – hAKR1B10 + NADP + caffeic acid ester<br /> | ||
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**[[2fvl]] – hAKR1C4 + NADP <br /> | **[[2fvl]] – hAKR1C4 + NADP <br /> | ||
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| + | *AKR1C13 | ||
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| + | **[[6m7k]] – AKR1C13 + cyclic AMP-AMP-GMP - mouse<br /> | ||
*AKR1C21 or 17-alpha hydroxysteroid dehydrogenase See [[Hydroxysteroid dehydrogenase]] 17-alpha HSD | *AKR1C21 or 17-alpha hydroxysteroid dehydrogenase See [[Hydroxysteroid dehydrogenase]] 17-alpha HSD | ||
Revision as of 10:28, 4 March 2019
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3D structures of aldo-keto reductase
Updated on 04-March-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
