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Fructose-1,6-bisphosphatase

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== Structural highlights ==
== Structural highlights ==
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A tricyclic potent FBP inhibitor interacts with the enzyme in a hydrophobic pocket <ref>PMID:20045638</ref>.
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A <scene name='46/468243/Cv/4'>tricyclic potent FBP inhibitor interacts with the enzyme in a hydrophobic pocket</scene> <ref>PMID:20045638</ref> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}).
</StructureSection>
</StructureSection>

Revision as of 14:36, 3 March 2016

Human liver fructose-1,6-bisphosphatase complex with inhibitor (PDB entry 3kc0)

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3D Structures of Fructose-1,6-bisphosphatase

Updated on 03-March-2016

References

  1. Zhang Y, Liang JY, Lipscomb WN. Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase. Biochem Biophys Res Commun. 1993 Feb 15;190(3):1080-3. PMID:8382485
  2. Storey KB. Metabolic regulation in mammalian hibernation: enzyme and protein adaptations. Comp Biochem Physiol A Physiol. 1997 Dec;118(4):1115-24. PMID:9505421
  3. van Poelje PD, Potter SC, Chandramouli VC, Landau BR, Dang Q, Erion MD. Inhibition of fructose 1,6-bisphosphatase reduces excessive endogenous glucose production and attenuates hyperglycemia in Zucker diabetic fatty rats. Diabetes. 2006 Jun;55(6):1747-54. PMID:16731838 doi:http://dx.doi.org/10.2337/db05-1443
  4. van Poelje PD, Potter SC, Erion MD. Fructose-1, 6-bisphosphatase inhibitors for reducing excessive endogenous glucose production in type 2 diabetes. Handb Exp Pharmacol. 2011;(203):279-301. doi: 10.1007/978-3-642-17214-4_12. PMID:21484576 doi:http://dx.doi.org/10.1007/978-3-642-17214-4_12
  5. Tsukada T, Takahashi M, Takemoto T, Kanno O, Yamane T, Kawamura S, Nishi T. Structure-based drug design of tricyclic 8H-indeno[1,2-d][1,3]thiazoles as potent FBPase inhibitors. Bioorg Med Chem Lett. 2010 Feb 1;20(3):1004-7. Epub 2009 Dec 21. PMID:20045638 doi:10.1016/j.bmcl.2009.12.056

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Michal Harel, Alexander Berchansky

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