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Séminaire IBMM

Investigating the selectivity of human cytosolic sulfotransferases SULT1A1 and SULT1A3 : a computational and experimental study

Dr. Larryn Peterson (Rhodes College, Memphis, TN, USA)

publié le

Le Jeudi 30 Mai 2013 à 16h00
ENSCM, salle de conférences Recherche (Bâtiment Max Mousseron, 4ee étage), 8 rue de l’école normale, Montpellier)

Cytosolic SULTs catalyze the transfer of a sulfuryl moiety (-SO3) from the activated sulfate (3’-phosphoadenosine-5’-phosphosulfate ; PAPS) to an acceptor (usually an ROH or ArOH). SULTs play an important role in the regulation of the levels and activities of neurotransmitters and hormones, as well as the excretion of xenobiotics. To date, 13 human cytosolic SULTs have been identified. Though the family members share considerable sequence and structural similarity, they appear to have dissimilar biological functions. For example, SULT1A1 readily sulfates simple phenols, such as para-nitrophenol (pNP) and 1-naphthol, whereas SULT1A3 has strong affinity for catecholamines, such as dopamine and norepinephrine, and weaker affinity for pNP and 1-naphthol. The basis of this selectivity is not well understood. To elucidate the molecular basis for substrate selectivity and specificity, we have taken a combined computational and experimental approach by identifying key protein-ligand interactions using in silico modeling, synthesizing a series of analogues, and evaluating the biological activity of these compounds in an enzymatic assay. The molecular modeling of select pNP and dopamine analogues bound in the active site of SULT1A1 and SULT1A3 and the synthesis of the analogous compounds will be discussed.

Contact local IBMM : Dr. Sébastien Ulrich (équipe Glycochimie Reconnaissance Moléculaire)


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