A synthetic lectin for O-linked beta-N-acetylglucosamine.
Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-GlcNAc) up to 100 times more strongly than it does glucose. This synthetic lectin shows affinities similar to wheat germ agglutinin (WGA), a natural lectin used to bind GlcNAc. Remarkably, 1 is more selective than WGA. It favors especially the glycoside unit in glycopeptide 2, a model of the serine-O-GlcNAc posttranslational protein modification.
Ferrand
Yann
Y
School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Klein
Emmanuel
E
Barwell
Nicholas P
NP
Crump
Matthew P
MP
Jiménez-Barbero
Jesus
J
Vicent
Cristina
C
Boons
Geert-Jan
GJ
Ingale
Sampat
S
Davis
Anthony P
AP
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000737:chemistry; D007700:Kinetics; D037102:Lectins / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D011499:Protein Processing, Post-Translational; D014909:Wheat Germ Agglutinins / Q000378:metabolism
D002241:Carbohydrates; D037102:Lectins; D014909:Wheat Germ Agglutinins; D000117:Acetylglucosamine