Journal
EMBO JOURNAL
Volume 19, Issue 4, Pages 581-588Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.4.581
Keywords
class I alpha 1,2-mannosidase; crystallography; drug design; ER quality control; processing glycosidase
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Funding
- NIGMS NIH HHS [R01 GM031265, GM 31265] Funding Source: Medline
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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 alpha 1,2-mannosidase that trims Man(9)GlcNAc(2) to Man(8)GlcNAc(2) isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (alpha alpha)(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.
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