4ju5: Difference between revisions
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{{STRUCTURE_4ju5| PDB=4ju5 | SCENE= }} | |||
===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase=== | |||
==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== | |||
[[4ju5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JU5 OCA]. | |||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Protein disulfide-isomerase]] | |||
[[Category: Bastos-Aristizabal, S.]] | |||
[[Category: Gehring, K.]] | |||
[[Category: Kozlov, G.]] | |||
[[Category: Chaperone]] | |||
[[Category: Disulfide isomerase]] | |||
[[Category: Isomerase]] | |||
[[Category: Thioredoxin-like fold]] | |||
Revision as of 17:47, 19 February 2014
Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase
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
- ↑ 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
