Tyrosylprotein sulfotransferase inhibitors generated by combinatorial target-guided ligand assembly.
Tyrosylprotein sulfotransferases (TPSTs) catalyze the sulfation of tyrosine residues within secreted and membrane-bound proteins. The modification modulates protein-protein interactions in the extracellular environment. Here we use combinatorial target-guided ligand assembly to discover the first known inhibitors of human TPST-2.
Kehoe
John W
JW
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Maly
Dustin J
DJ
Verdugo
Dawn E
DE
Armstrong
Joshua I
JI
Cook
Brian N
BN
Ouyang
Ying-Bin
YB
Moore
Kevin L
KL
Ellman
Jonathan A
JA
Bertozzi
Carolyn R
CR
D000447:Aldehydes / Q000737:chemistry; D020650:Combinatorial Chemistry Techniques; D003600:Cytosol / Q000187:drug effects / Q000201:enzymology; D004353:Drug Evaluation, Preclinical; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D007202:Indicators and Reagents; D008024:Ligands; D015238:Sulfotransferases / Q000037:antagonists & inhibitors*
D000447:Aldehydes; D004791:Enzyme Inhibitors; D007202:Indicators and Reagents; D008024:Ligands; D015238:Sulfotransferases; C039079:protein-tyrosine sulfotransferase; C020122:estrone sulfotransferase