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- Title
Crystal structure of a class I a1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control.
- Authors
Vallée, François; Lipari, Francesco; Yip, Patrick; Sleno, Barry; Herscovics, Annette; Howell, P. Lynne
- Abstract
Mannose trimming is not only essential for N-glycan maturation in mammalian cells but also triggers degradation of misfolded glycoproteins. The crystal structure of the class I α1,2-mannosidase that trims MangGlcNAc2 to Man8GlcNAc2 isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (αα)7-barrel in which an N-glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion. The observed protein-carbohydrate interactions provide the first insight into the catalytic mechanism and specificity of this eukaryotic enzyme family and may be used to design inhibitors that prevent degradation of misfolded glycoproteins in genetic diseases.
- Subjects
MANNOSIDASES; GLYCOSIDASES; GLYCOPROTEINS; DRUG design; ENDOPLASMIC reticulum; SACCHAROMYCES cerevisiae; CRYSTALLOGRAPHY; BIOCHEMISTRY; MOLECULAR biology
- Publication
EMBO Journal, 2000, Vol 19, Issue 4, p581
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/19.4.581