ERp27 (Endoplasmic Reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase), localised to the Endoplasmic Reticulum. The structure of ERp27 has been solved by both X-ray crystallography and NMR spectroscopy, showing it to be composed of two thioredoxin-like domains with homology to the non-catalytic b and b' domains of PDI. The function of ERp27 is unknown, but on the basis of its homology with PDI it is thought to possess chaperone activity.
References
- Kober FX, Koelmel W, Kuper J, Drechsler J, Mais C, Hermanns HM, Schindelin H, The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities. J Biol Chem. 2013 Jan 18;288(3):2029-39
- Amin NT, Wallis AK, Wells SA, Rowe ML, Williamson RA, Howard MJ, Freedman RB, High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility. Biochem J. 2013 Mar 1;450(2):321-32
- Galligan JJ, Petersen DR (July 2012). "The human protein disulfide isomerase gene family". Human Genomics. 6 (6): 6. doi:10.1186/1479-7364-6-6. PMC 3500226. PMID 23245351.
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