1G7E

NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN

Summary for 1G7E

• Entry DOI: 10.2210/pdb1g7e/pdb
• Related: 1G7D
• NMR Information: BMRB: 4919
• Descriptor: ENDOPLASMIC RETICULUM PROTEIN ERP29 (1 entity in total)
• Functional Keywords: alfa-beta structure, thioredoxin fold, chaperone
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 13874.75

Authors

Liepinsh, E.,Mkrtchian, S.,Barishev, M.,Sharipo, M.,Ingelman-Sundberg, M.,Otting, G. (deposition date: 2000-11-10, release date: 2000-11-29, Last modification date: 2024-05-22)

Primary citation

Liepinsh, E.,Baryshev, M.,Sharipo, A.,Ingelman-Sundberg, M.,Otting, G.,Mkrtchian, S.
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.
Structure, 9:457-471, 2001

PubMed Abstract: 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.

PubMed: 11435111
DOI: 10.1016/S0969-2126(01)00607-4

Experimental method

SOLUTION NMR