4ekz | pdb_00004ekz
Crystal structure of reduced hPDI (abb'xa')
Template:ABSTRACT PUBMED 22657537
Function
[PDIA1_HUMAN] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.[1] [2]
About this Structure
4ekz is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Wang C, Li W, Ren J, Fang J, Ke H, Gong W, Feng W, Wang CC. Structural Insights into the Redox-Regulated Dynamic Conformations of Human Protein Disulfide Isomerase. Antioxid Redox Signal. 2012 Jul 9. PMID:22657537 doi:10.1089/ars.2012.4630
- ↑ Mezghrani A, Courageot J, Mani JC, Pugniere M, Bastiani P, Miquelis R. Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes. J Biol Chem. 2000 Jan 21;275(3):1920-9. PMID:10636893
- ↑ Lumb RA, Bulleid NJ. Is protein disulfide isomerase a redox-dependent molecular chaperone? EMBO J. 2002 Dec 16;21(24):6763-70. PMID:12485997
