1dl2
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(New page: 200px<br /><applet load="1dl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dl2, resolution 1.54Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 11:15, 20 November 2007
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CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION
Overview
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 alpha1, 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 (alphaalpha)(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.
About this Structure
1DL2 is a Single protein structure of sequence from Saccharomyces cerevisiae with NAG, CA and GOL as ligands. Active as Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113 Full crystallographic information is available from OCA.
Reference
Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control., Vallee F, Lipari F, Yip P, Sleno B, Herscovics A, Howell PL, EMBO J. 2000 Feb 15;19(4):581-8. PMID:10675327
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