Molecular Playground/ERMan1: Difference between revisions

New page: ==This is a placeholder== Alpha-mannosidases I(ERMan1) is a human protein that reside in the endoplasmic reticulum(ER) lumen. ERMan1 is part of the class 1 glycosylhydrolase family 47 grou...
 
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==This is a placeholder==
==ERMan1==
Alpha-mannosidases I(ERMan1) is a human protein that reside in the endoplasmic reticulum(ER) lumen. ERMan1 is part of the class 1 glycosylhydrolase family 47 group of proteins and sports a Tim-barrel fold. In the ER N-linked glycans are used as indicators of how well a client protein is folded. ERMan1 functions by slowly trimming N-linked glycans, giving the protein at hand a defined window of time before the client protein can be targeted for degradation by other ER proteins.  
Alpha-mannosidases I(ERMan1) is a human protein that resides in the endoplasmic reticulum(ER). ERMan1 is a member of the class 1 glycosylhydrolase family 47 group proteins and sports a Tim-barrel fold. Asparagine(N)-linked glycans are common covalent modifiers in the ER that aid in protein folding and trafficking. ERMan1 trims N-linked glycans to target a misfolded protein for degradation. The slow acting kinetics of ERMan1 have been proposed to act as a timer for protein degradation, creating a discrete window for protein folding followed by degradation if the substrate protein cannot reach the native state.  






{{STRUCTURE_1x9d |  PDB=1x9d  |  SCENE=  }}




{{STRUCTURE_1x9d|  PDB=1x9d  | SIZE=300| SCENE= |right|  CAPTION=Human α-mannosidase class I complex with mannopyranoside, sulfate, 1,4-butanediol, Ca+2 ion, [[1x9d]] }}


"Molecular Playground banner: A catalytic timer for protein degradation."
"Molecular Playground banner: A catalytic timer for protein degradation."
==3D structures of mannosidases==
[[Mannosidase]]


[http://proteopedia.org/wiki/index.php/CBI_Molecules]
[http://proteopedia.org/wiki/index.php/CBI_Molecules]
[http://proteopedia.org/wiki/index.php/1x9d]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Johan Sunryd, Michal Harel