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3uem
From Proteopedia
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{{STRUCTURE_3uem| PDB=3uem | SCENE= }} | {{STRUCTURE_3uem| PDB=3uem | SCENE= }} | ||
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===Crystal structure of human PDI bb'a' domains=== | ===Crystal structure of human PDI bb'a' domains=== | ||
| + | {{ABSTRACT_PUBMED_22090031}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PDIA1_HUMAN 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.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[3uem]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEM OCA]. | [[3uem]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEM OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:022090031</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
Revision as of 07:12, 30 June 2013
Contents |
Crystal structure of human PDI bb'a' domains
Template:ABSTRACT PUBMED 22090031
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
3uem is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Wang C, Yu J, Huo L, Wang L, Feng W, Wang CC. Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'. J Biol Chem. 2012 Jan 6;287(2):1139-49. Epub 2011 Nov 16. PMID:22090031 doi:10.1074/jbc.M111.303149
- ↑ 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
