4ekz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 7: Line 7:


==About this Structure==
==About this Structure==
[[4ekz]] 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=4EKZ OCA].  
[[4ekz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKZ OCA].  


==Reference==
==Reference==
<references group="xtra"/><references/>
<ref group="xtra">PMID:022657537</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Protein disulfide-isomerase]]
[[Category: Protein disulfide-isomerase]]
[[Category: Feng, W.]]
[[Category: Feng, W.]]

Revision as of 11:28, 3 July 2013

Template:STRUCTURE 4ekz

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. Full crystallographic information is available from OCA.

Reference

  1. 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
  1. ↑ 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
  2. ↑ Lumb RA, Bulleid NJ. Is protein disulfide isomerase a redox-dependent molecular chaperone? EMBO J. 2002 Dec 16;21(24):6763-70. PMID:12485997

Proteopedia Page Contributors and Editors (what is this?)

OCA