4ju5

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'''Unreleased structure'''
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{{STRUCTURE_4ju5| PDB=4ju5 | SCENE= }}
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===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===
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The entry 4ju5 is ON HOLD until Paper Publication
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==Function==
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[[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>
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Authors: Bastos-Aristizabal, S., Kozlov, G., Gehring, K.
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==About this Structure==
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[[4ju5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JU5 OCA].
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Description: Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Protein disulfide-isomerase]]
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[[Category: Bastos-Aristizabal, S.]]
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[[Category: Gehring, K.]]
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[[Category: Kozlov, G.]]
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[[Category: Chaperone]]
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[[Category: Disulfide isomerase]]
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[[Category: Isomerase]]
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[[Category: Thioredoxin-like fold]]

Revision as of 17:47, 19 February 2014

Template:STRUCTURE 4ju5

Contents

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

  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

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