4ekz

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'''Unreleased structure'''
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{{STRUCTURE_4ekz| PDB=4ekz | SCENE= }}
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===Crystal structure of reduced hPDI (abb'xa')===
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{{ABSTRACT_PUBMED_22657537}}
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The entry 4ekz is ON HOLD until Apr 10 2014
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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: Wang, C., Li, W., Ren, J., Ke, H., Gong, W., Feng, W., Wang, C.-C.
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==About this Structure==
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[[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].
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Description: Crystal structure of reduced hPDI (abb'xa')
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Protein disulfide-isomerase]]
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[[Category: Feng, W.]]
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[[Category: Gong, W.]]
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[[Category: Ke, H.]]
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[[Category: Li, W.]]
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[[Category: Ren, J.]]
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[[Category: Wang, C.]]
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[[Category: Wang, C C.]]
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[[Category: Cghc active site]]
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[[Category: A redox-regulated chaperone]]
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[[Category: Abb'a' domain]]
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[[Category: An enzyme]]
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[[Category: Chaperone]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Horseshoe shape]]

Revision as of 22:41, 10 April 2013

Template:STRUCTURE 4ekz

Contents

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 with sequence from Homo sapiens. 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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