Structural highlights
Function
ALDR_HUMAN Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Publication Abstract from PubMed
The effect of halogen-to-hydrogen bond substitution on the binding energetics and biological activity of a human aldose reductase inhibitor has been studied using X-ray crystallography, IC50 measurements, advanced binding free energy calculations, and simulations. The replacement of Br or I atoms by an amine (NH2) group has not induced changes in the original geometry of the complex, which made it possible to study the isolated features of selected noncovalent interactions in a biomolecular complex.
The Effect of Halogen-to-Hydrogen Bond Substitution on Human Aldose Reductase Inhibition.,Fanfrlik J, Ruiz FX, Kadlcikova A, Rezac J, Cousido-Siah A, Mitschler A, Haldar S, Lepsik M, Kolar MH, Majer P, Podjarny AD, Hobza P ACS Chem Biol. 2015 Jul 17;10(7):1637-42. doi: 10.1021/acschembio.5b00151. Epub, 2015 May 6. PMID:25919404[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fanfrlik J, Ruiz FX, Kadlcikova A, Rezac J, Cousido-Siah A, Mitschler A, Haldar S, Lepsik M, Kolar MH, Majer P, Podjarny AD, Hobza P. The Effect of Halogen-to-Hydrogen Bond Substitution on Human Aldose Reductase Inhibition. ACS Chem Biol. 2015 Jul 17;10(7):1637-42. doi: 10.1021/acschembio.5b00151. Epub, 2015 May 6. PMID:25919404 doi:http://dx.doi.org/10.1021/acschembio.5b00151
