4ju5
From Proteopedia
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{{STRUCTURE_4ju5| PDB=4ju5 | SCENE= }} | {{STRUCTURE_4ju5| PDB=4ju5 | SCENE= }} | ||
===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase=== | ===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase=== | ||
| + | {{ABSTRACT_PUBMED_24549644}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
| - | <references group="xtra"/><references/> | + | <ref group="xtra">PMID:024549644</ref><references group="xtra"/><references/> |
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
[[Category: Bastos-Aristizabal, S.]] | [[Category: Bastos-Aristizabal, S.]] | ||
Revision as of 09:12, 19 March 2014
Contents |
Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase
Template:ABSTRACT PUBMED 24549644
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
4ju5 is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Bastos-Aristizabal S, Kozlov G, Gehring K. Structural insight into the dimerization of human protein disulfide isomerase. Protein Sci. 2014 Feb 18. doi: 10.1002/pro.2444. PMID:24549644 doi:http://dx.doi.org/10.1002/pro.2444
- ↑ 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
