1GYA

N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2

Summary for 1GYA

• Entry DOI: 10.2210/pdb1gya/pdb
• Descriptor: HUMAN CD2, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: cell surface adhesion receptor, immunoglobulin superfamily v-set domain, t lymphocyte adhesion glycoprotein, adhesion glycoprotein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 14012.60

Authors

Wyss, D.F.,Choi, J.S.,Wagner, G. (deposition date: 1995-05-26, release date: 1996-11-08, Last modification date: 2024-10-09)

Primary citation

Wyss, D.F.,Choi, J.S.,Li, J.,Knoppers, M.H.,Willis, K.J.,Arulanandam, A.R.,Smolyar, A.,Reinherz, E.L.,Wagner, G.
Conformation and function of the N-linked glycan in the adhesion domain of human CD2.
Science, 269:1273-1278, 1995

PubMed Abstract: 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.

PubMed: 7544493

Experimental method

SOLUTION NMR