3w8j

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'''Unreleased structure'''
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{{STRUCTURE_3w8j| PDB=3w8j | SCENE= }}
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===Crystal structure of P5 a0 in a complex with Prx4 c-term===
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{{ABSTRACT_PUBMED_23949117}}
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The entry 3w8j is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN]] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref> [[http://www.uniprot.org/uniprot/PRDX4_MOUSE PRDX4_MOUSE]] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
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Authors: Inaba, K., Suzuki, M., Kojima, R.
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==About this Structure==
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[[3w8j]] is a 4 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=3W8J OCA].
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Description: Crystal structure of P5 a0 in a complex with Prx4 c-term
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==Reference==
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<ref group="xtra">PMID:023949117</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Protein disulfide-isomerase]]
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[[Category: Inaba, K.]]
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[[Category: Kojima, R.]]
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[[Category: Suzuki, M.]]
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[[Category: Oxidoreductase-isomerase complex]]
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[[Category: Pdi family member]]
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[[Category: Protein disulfide isomerase]]
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[[Category: Thioredoxin fold]]

Revision as of 10:45, 4 September 2013

Template:STRUCTURE 3w8j

Contents

Crystal structure of P5 a0 in a complex with Prx4 c-term

Template:ABSTRACT PUBMED 23949117

Function

[PDIA6_HUMAN] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.[1] [2] [PRDX4_MOUSE] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

About this Structure

3w8j is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. Sci Rep. 2013 Aug 16;3:2456. doi: 10.1038/srep02456. PMID:23949117 doi:10.1038/srep02456
  1. ↑ Jordan PA, Stevens JM, Hubbard GP, Barrett NE, Sage T, Authi KS, Gibbins JM. A role for the thiol isomerase protein ERP5 in platelet function. Blood. 2005 Feb 15;105(4):1500-7. Epub 2004 Oct 5. PMID:15466936 doi:10.1182/blood-2004-02-0608
  2. ↑ Kikuchi M, Doi E, Tsujimoto I, Horibe T, Tsujimoto Y. Functional analysis of human P5, a protein disulfide isomerase homologue. J Biochem. 2002 Sep;132(3):451-5. PMID:12204115

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