Publication Date:
1995-09-01
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyss, D F -- Choi, J S -- Li, J -- Knoppers, M H -- Willis, K J -- Arulanandam, A R -- Smolyar, A -- Reinherz, E L -- Wagner, G -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1273-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7544493" target="_blank"〉PubMed〈/a〉
Keywords:
Acetylglucosamine/chemistry
;
Amino Acid Sequence
;
Animals
;
Antigens, CD/metabolism
;
Antigens, CD2/*chemistry/metabolism
;
Antigens, CD58
;
Binding Sites
;
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
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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