The structure of calnexin, an ER chaperone involved in quality control of protein folding

被引：312

作者：

Schrag, JD

Bergeron, JJM

Li, YG

Borisova, S

Hahn, M

Thomas, DY

Cygler, M

机构：

[1] Natl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, Canada

[2] McGill Univ, Dept Anat & Cell Biol, Montreal, PQ H3A 2T5, Canada

来源：

MOLECULAR CELL | 2001年 / 8卷 / 03期

基金：

加拿大健康研究院;

关键词：

D O I：

10.1016/S1097-2765(01)00318-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 Angstrom resolution reveals an extended 140 Angstrom arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich sequence motifs which interact with one another in a head-to-tail fashion. Identification of the ligand binding site establishes calnexin as a monovalent lectin, providing insight into the mechanism by which the calnexin family of chaperones interacts with monoglucosylated glycoproteins.

引用

收藏

页码：633 / 644

页数：12

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