Conformation and function of the N-linked glycan in the adhesion domain of human CD2

Science. 1995 Sep 1;269(5228):1273-8. doi: 10.1126/science.7544493.


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-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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylglucosamine / chemistry
  • Amino Acid Sequence
  • Animals
  • Antigens, CD / metabolism
  • Binding Sites
  • CD2 Antigens / chemistry*
  • CD2 Antigens / metabolism
  • CD58 Antigens
  • CHO Cells
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cell Adhesion
  • Cricetinae
  • Glycosylation
  • Humans
  • Magnetic Resonance Spectroscopy
  • Membrane Glycoproteins / metabolism
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oligosaccharides / chemistry*
  • Protein Conformation*


  • Antigens, CD
  • CD2 Antigens
  • CD58 Antigens
  • Membrane Glycoproteins
  • Oligosaccharides
  • Acetylglucosamine