D
David K. Wilson
Researcher at University of California, Davis
Publications - 59
Citations - 3436
David K. Wilson is an academic researcher from University of California, Davis. The author has contributed to research in topics: Active site & Aldo-keto reductase. The author has an hindex of 31, co-authored 59 publications receiving 3288 citations. Previous affiliations of David K. Wilson include Baylor College of Medicine & Washington University in St. Louis.
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Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations
TL;DR: A stereoselective addition-elimination or SN2 mechanism of the enzyme is proposed with the zinc atom and the Glu and Asp residues playing key roles and a molecular explanation of a hereditary disease caused by several point mutations of an enzyme is presented.
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An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications
TL;DR: The structure of a recombinant human placenta aldose reductase is refined and it is revealed that the enzyme contains a parallel beta 8/alpha 8-barrel motif and establishes a new motif for NADP-binding oxidoreductases.
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Substrate specificity and affinity of a protein modulated by bound water molecules
TL;DR: Evidence is presented that bound water molecules, coupled with localized conformational changes, can govern substrate specificity and affinity in the complexes of the L-arabinose-binding protein with D-fucose and D-galactose, to illustrate how ordered water molecules can contribute directly to the properties of proteins by influencing their interaction with ligands.
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Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.
TL;DR: The refined 1.1.8 A x-ray structure of the human holoenzyme complexed with zopolrestat, one of the most potent noncompetitive inhibitors, is reported, key to understanding the mode of action of this class of inhibitors and for rational design of better therapeutics.
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The crystal structure of an odorant binding protein from Anopheles gambiae: Evidence for a common ligand release mechanism.
TL;DR: It is demonstrated that AgamOBP1 undergoes a pH dependent conformational change that is associated with reduced ligand binding, and this results suggest a common mechanism for OBP activity.