1GYA

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

1GYA の概要

• エントリーDOI: 10.2210/pdb1gya/pdb
• 分子名称: 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)
• 機能のキーワード: cell surface adhesion receptor, immunoglobulin superfamily v-set domain, t lymphocyte adhesion glycoprotein, adhesion glycoprotein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14012.60

構造登録者

Wyss, D.F.,Choi, J.S.,Wagner, G. (登録日: 1995-05-26, 公開日: 1996-11-08, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

SOLUTION NMR