1g7d
From Proteopedia
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'''NMR STRUCTURE OF ERP29 C-DOMAIN''' | '''NMR STRUCTURE OF ERP29 C-DOMAIN''' | ||
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[[Category: Otting, G.]] | [[Category: Otting, G.]] | ||
[[Category: Sharipo, A.]] | [[Category: Sharipo, A.]] | ||
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Revision as of 14:14, 2 May 2008
NMR STRUCTURE OF ERP29 C-DOMAIN
Overview
BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers. RESULTS: 3D structures of the N- and C-terminal domains determined by NMR spectroscopy confirmed the thioredoxin fold for the N-terminal domain and yielded a novel all-helical fold for the C-terminal domain. Studies of the full-length protein revealed a short, flexible linker between the two domains, homodimerization by the N-terminal domain, and the presence of interaction sites for the formation of higher molecular weight oligomers. A gadolinium-based relaxation agent is shown to present a sensitive tool for the identification of macromolecular interfaces by NMR. CONCLUSIONS: ERp29 is the first eukaryotic PDI-related protein for which the structures of all domains have been determined. Furthermore, an experimental model of the full-length protein and its association states was established. It is the first example of a protein where the thioredoxin fold was found to act as a specific homodimerization module, without covalent linkages or supporting interactions by further domains. A homodimerization module similar as in ERp29 may also be present in homodimeric human PDI.
About this Structure
1G7D is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer., Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S, Structure. 2001 Jun;9(6):457-71. PMID:11435111 Page seeded by OCA on Fri May 2 17:13:58 2008
