ERp27

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,^[1]^[2] 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.^[3]

References[edit]

^ 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.

This protein-related article is a stub. You can help Wikipedia by expanding it.

[1] 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

[2] 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

[humgenomics.com-3] 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.

[1]

[2]

[3]