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1g7d
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(New page: 200px<br /><applet load="1g7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g7d" /> '''NMR STRUCTURE OF ERP29 C-DOMAIN'''<br /> ==...)
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Revision as of 13:39, 20 November 2007
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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
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