Molecular Playground/Hsp70-Hsp90: Difference between revisions
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==Hsp-70-Hsp-90 Organizing Protein== | ==Hsp-70-Hsp-90 Organizing Protein== | ||
==TPR Domain 1 Structure== | |||
<scene name='User:Lydia_Lamriben/Sandbox1/Erdj5/1'>ERdj5</scene> is an Endoplasmic Reticulum (ER) resident protein disulfide isomerase. It is a 793 amino acid multi-domain protein. It consists of an N-terminal <scene name='User:Lydia_Lamriben/Sandbox1/J-domain/4'>J-domain</scene> that has been shown to bind to BIP, ER resident HSP70, four redox-active <scene name='User:Lydia_Lamriben/Sandbox1/Thioredoxin_domains/1'>thioredoxin</scene> domains (displayed here in green) and their respective redox-active CXXC motifs labeled in red and two <scene name='User:Lydia_Lamriben/Sandbox1/Thioredoxin-like_domains/3'>thioredoxin-like</scene> domains shown in yellow, which lack CXXC redox-active motifs. | <scene name='User:Lydia_Lamriben/Sandbox1/Erdj5/1'>ERdj5</scene> is an Endoplasmic Reticulum (ER) resident protein disulfide isomerase. It is a 793 amino acid multi-domain protein. It consists of an N-terminal <scene name='User:Lydia_Lamriben/Sandbox1/J-domain/4'>J-domain</scene> that has been shown to bind to BIP, ER resident HSP70, four redox-active <scene name='User:Lydia_Lamriben/Sandbox1/Thioredoxin_domains/1'>thioredoxin</scene> domains (displayed here in green) and their respective redox-active CXXC motifs labeled in red and two <scene name='User:Lydia_Lamriben/Sandbox1/Thioredoxin-like_domains/3'>thioredoxin-like</scene> domains shown in yellow, which lack CXXC redox-active motifs. | ||
Revision as of 23:51, 3 December 2013
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Hsp-70-Hsp-90 Organizing ProteinHsp-70-Hsp-90 Organizing Protein
TPR Domain 1 StructureTPR Domain 1 Structure
is an Endoplasmic Reticulum (ER) resident protein disulfide isomerase. It is a 793 amino acid multi-domain protein. It consists of an N-terminal that has been shown to bind to BIP, ER resident HSP70, four redox-active domains (displayed here in green) and their respective redox-active CXXC motifs labeled in red and two domains shown in yellow, which lack CXXC redox-active motifs.
FunctionFunction
ERdj5 is believed to play a critical role in ERAD (ER Associated Degradation) in that it is required for reducing ERAD substrates and facilitating their retrotranslocation from the ER to the cytoplasm. It has been shown to interact with EDEM (ER Degradation Enhancing Mannosidase), a protein that recognizes misfolded substrates and targets them for ERAD.
ReferencesReferences
1. Hagiwara M. et. al. Molecular Cell; 41. 2011
2. Ushioda R. et. al. Science; 321. 2008