Conformation and function of the N-linked glycan in the adhesion domain of human CD2
DF Wyss, JS Choi, J Li, MH Knoppers, KJ Willis… - Science, 1995 - science.org
DF Wyss, JS Choi, J Li, MH Knoppers, KJ Willis, ARN Arulanandam, A Smolyar, EL Reinherz…
Science, 1995•science.orgThe adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution
structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-
(NN-acetylglucosamine) 2-(mannose) 5-8] was solved by nuclear magnetic resonance. The
stem and two of three branches of the carbohydrate structure are well defined and the
mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of
the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather …
structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-
(NN-acetylglucosamine) 2-(mannose) 5-8] was solved by nuclear magnetic resonance. The
stem and two of three branches of the carbohydrate structure are well defined and the
mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of
the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather …
The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N- N-acetylglucosamine)2-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2.
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