1g7d

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{{STRUCTURE_1g7d| PDB=1g7d | SCENE= }}
{{STRUCTURE_1g7d| PDB=1g7d | SCENE= }}
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'''NMR STRUCTURE OF ERP29 C-DOMAIN'''
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===NMR STRUCTURE OF ERP29 C-DOMAIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11435111 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11435111}}
==About this Structure==
==About this Structure==
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1G7D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].
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1G7D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].
==Reference==
==Reference==
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[[Category: Sharipo, A.]]
[[Category: Sharipo, A.]]
[[Category: Alpha helical protein]]
[[Category: Alpha helical protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:49:26 2008''

Revision as of 01:49, 1 July 2008

Image:1g7d.png

Template:STRUCTURE 1g7d

NMR STRUCTURE OF ERP29 C-DOMAIN

Template:ABSTRACT PUBMED 11435111

About this Structure

1G7D is a Single protein structure of sequence from Rattus norvegicus. Full experimental 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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