Probing the extended binding determinants of oligosaccharyl transferase with synthetic inhibitors of asparagine-linked glycosylation.
Protein glycosylation is associated with many critical biological processes. In connection with studies on the mechanism of asparagine-linked glycosylation by the enzyme oligosaccharyl transferase, we have prepared peptide inhibitors that interact with the enzyme at nanomolar concentrations. Herein we describe efforts directed toward improving the binding properties of these inhibitors.
de L Ufret
M
M
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA.
Imperiali
B
B
D000595:Amino Acid Sequence; D001216:Asparagine / Q000378:metabolism*; D006031:Glycosylation; D006602:Hexosyltransferases; D008565:Membrane Proteins; D015335:Molecular Probes; D013379:Substrate Specificity; D014166:Transferases / Q000378:metabolism*
D008565:Membrane Proteins; D015335:Molecular Probes; D001216:Asparagine; D014166:Transferases; D006602:Hexosyltransferases; C025620:dolichyl-diphosphooligosaccharide - protein glycotransferase