1g7e: Difference between revisions

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[[Image:1g7e.gif|left|200px]]
{{Seed}}
[[Image:1g7e.png|left|200px]]


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{{STRUCTURE_1g7e|  PDB=1g7e  |  SCENE=  }}  
{{STRUCTURE_1g7e|  PDB=1g7e  |  SCENE=  }}  


'''NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN'''
===NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN===




==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==
1G7E 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=1G7E OCA].  
1G7E 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=1G7E OCA].  


==Reference==
==Reference==
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[[Category: Alfa-beta structure]]
[[Category: Alfa-beta structure]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:49:27 2008''

Revision as of 01:49, 1 July 2008

File:1g7e.png

Template:STRUCTURE 1g7e

NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN

Template:ABSTRACT PUBMED 11435111

About this Structure

1G7E 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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