Journal
EMBO REPORTS
Volume 9, Issue 7, Pages 642-647Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/embor.2008.88
Keywords
chaperone; crystallography; ERp44; PDI family; quality control
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Funding
- Associazione Italiana per la Ricerca sul Cancro Funding Source: Custom
- Telethon [GGP06155] Funding Source: Medline
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ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 angstrom. Three thioredoxin domains-a, b and b'-are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b' and a domains, shielding a hydrophobic pocket in domain b' and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional studies indicate that the C-terminal tail gates the CRFS area and the adjacent hydrophobic pocket, dynamically regulating protein quality control.
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