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Comparison of crystal structures of human androgen receptor ligand‐binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity
Androgens exert their effects by binding to the highly specific androgen receptor (AR). In addition to natural potent androgens, AR binds a variety of synthetic agonist or antagonist molecules withExpand
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Multiple Conformers in Active Site of Human Dihydrofolate Reductase F31R/Q35E Double Mutant Suggest Structural Basis for Methotrexate Resistance*
Methotrexate is a slow, tight-binding, competitive inhibitor of human dihydrofolate reductase (hDHFR), an enzyme that provides key metabolites for nucleotide biosynthesis. In an effort to betterExpand
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Acidic residues on the voltage-sensor domain determine the activation of the NaChBac sodium channel.
The voltage-sensing domain of voltage-gated ion channels is characterized by specific, conserved, charged residues. Positively charged residues on segment S4 are the main contributors toExpand
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Accessibility of Four Arginine Residues on the S4 Segment of the Bacillus halodurans Sodium Channel
The voltage-gated Na+ channel of Bacillus halodurans (NaChBac) is composed of six transmembrane segments (S1–S6), with a pore-forming region composed of segments S5 and S6 and a voltage-sensingExpand
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Mapping of steroids binding to 17 beta-hydroxysteroid dehydrogenase type 1 using Monte Carlo energy minimization reveals alternative binding modes.
Crystallographic studies of ligand-protein complexes reveal most preferable ligand binding modes, but do not show less populated modes that may contribute to measurable biochemical and biophysicalExpand
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Un canal sans pore ? La structure primaire d’un canal perméable aux protons enfin dévoilée
930 canaux cationiques, la nature moleculaire des proteines responsables de ces conductances est demeuree longtemps obscure. Recemment, deux equipes (l’une japonaise et l’autre americaine) ontExpand
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  • Open Access
Role of juxtamembrane and transmembrane domains in the mechanism of natriuretic peptide receptor A activation.
Natriuretic peptide receptor A (NPRA) is a noncovalent homodimeric receptor, composed of an extracellular domain (ECD) with a ligand-binding site, a single transmembrane domain (TM), and anExpand
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