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TitleThioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.
Journal, issue, pagesStructure, Vol. 9, Page 457-471, Year 2001
Publish dateNov 10, 2000 (structure data deposition date)
AuthorsLiepinsh, E. / Baryshev, M. / Sharipo, A. / Ingelman-Sundberg, M. / Otting, G. / Mkrtchian, S.
External linksStructure / PubMed:11435111
MethodsNMR (solution)
Structure data

PDB-1g7d:
NMR STRUCTURE OF ERP29 C-DOMAIN
Method: SOLUTION NMR

PDB-1g7e:
NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN
Method: SOLUTION NMR

Source
  • rattus norvegicus (Norway rat)
KeywordsCHAPERONE / alpha helical protein / alfa-beta structure / thioredoxin fold

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