1dl2

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{{STRUCTURE_1dl2| PDB=1dl2 | SCENE= }}
{{STRUCTURE_1dl2| PDB=1dl2 | SCENE= }}
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'''CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION'''
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===CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION===
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==Overview==
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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 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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10675327 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10675327}}
==About this Structure==
==About this Structure==
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[[Category: Yip, P.]]
[[Category: Yip, P.]]
[[Category: Alpha-alpha helix barrel]]
[[Category: Alpha-alpha helix barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:14:01 2008''

Revision as of 20:14, 30 June 2008

Template:STRUCTURE 1dl2

CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 10675327

About this Structure

1DL2 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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