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”’ERp27”’ (Endoplasmic Reticulum protein 27.7 kDa) is a [[Sequence homology|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]],<ref>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</ref><ref>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</ref> 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.<ref name=”humgenomics.com”>{{cite journal | vauthors = Galligan JJ, Petersen DR | title = The human protein disulfide isomerase gene family | journal = Human Genomics | volume = 6 | issue = 6 | date = July 2012 | page = 6 | pmid = 23245351 | pmc = 3500226 | doi = 10.1186/1479-7364-6-6 | doi-access = free }}</ref> |
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ERp27(Endoplasmic Reticulum protein)encoded by TXNDC13 is a non-catalytic homologue of PDI (protein disulfide-isomerase), localized to the Endoplasmic Reticulum. Structural studies by X-ray crystallography and NMR have shown that ERp27 consists of two thioredoxin-like domains homologous to the b and b′ domains of PDI, and it lacks the catalytic Cys-X-X-Cys motif. Because it is non-enzymatic, ERp27 is known to function primarily in a chaperone-like role, although its precise biological function is still not fully defined. |
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==References== |
==References== |
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Latest revision as of 04:44, 2 December 2025
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]
- ^ 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.
