4ij3

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'''Unreleased structure'''
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{{STRUCTURE_4ij3| PDB=4ij3 | SCENE= }}
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===Oxidoreductase Fragment of Human QSOX1 in Complex with a FAB Fragment from an Anti- Human QSOX1 Antibody===
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{{ABSTRACT_PUBMED_23867277}}
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The entry 4ij3 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/QSOX1_HUMAN QSOX1_HUMAN]] Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation.<ref>PMID:16806532</ref> <ref>PMID:10542195</ref> <ref>PMID:10708601</ref> <ref>PMID:12176051</ref> <ref>PMID:17331072</ref> <ref>PMID:18393449</ref>
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Authors: Fass, D., Grossman, I.
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==About this Structure==
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[[4ij3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJ3 OCA].
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Description: Oxidoreductase Fragment of Human QSOX1 in Complex with a FAB Fragment from an Anti-Human QSOX1 Antibody
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==Reference==
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<ref group="xtra">PMID:023867277</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Mus musculus]]
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[[Category: Thiol oxidase]]
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[[Category: Fass, D.]]
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[[Category: Grossman, I.]]
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[[Category: Antibody binding]]
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[[Category: Inhibitor]]
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[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]

Revision as of 07:42, 6 November 2013

Template:STRUCTURE 4ij3

Contents

Oxidoreductase Fragment of Human QSOX1 in Complex with a FAB Fragment from an Anti- Human QSOX1 Antibody

Template:ABSTRACT PUBMED 23867277

Function

[QSOX1_HUMAN] Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation.[1] [2] [3] [4] [5] [6]

About this Structure

4ij3 is a 3 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

  • Grossman I, Alon A, Ilani T, Fass D. An Inhibitory Antibody Blocks the First Step in the Dithiol/Disulfide Relay Mechanism of the Enzyme QSOX1. J Mol Biol. 2013 Nov 15;425(22):4366-78. doi: 10.1016/j.jmb.2013.07.011. Epub, 2013 Jul 15. PMID:23867277 doi:http://dx.doi.org/10.1016/j.jmb.2013.07.011
  1. ↑ Radom J, Colin D, Thiebault F, Dognin-Bergeret M, Mairet-Coello G, Esnard-Feve A, Fellmann D, Jouvenot M. Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain. Biochim Biophys Acta. 2006 May;1759(5):225-33. Epub 2006 May 9. PMID:16806532 doi:http://dx.doi.org/10.1016/j.bbaexp.2006.04.008
  2. ↑ Hoober KL, Glynn NM, Burnside J, Coppock DL, Thorpe C. Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. J Biol Chem. 1999 Nov 5;274(45):31759-62. PMID:10542195
  3. ↑ Coppock D, Kopman C, Gudas J, Cina-Poppe DA. Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29. Biochem Biophys Res Commun. 2000 Mar 16;269(2):604-10. PMID:10708601 doi:http://dx.doi.org/10.1006/bbrc.2000.2324
  4. ↑ Thorpe C, Hoober KL, Raje S, Glynn NM, Burnside J, Turi GK, Coppock DL. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys. 2002 Sep 1;405(1):1-12. PMID:12176051
  5. ↑ Chakravarthi S, Jessop CE, Willer M, Stirling CJ, Bulleid NJ. Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Biochem J. 2007 Jun 15;404(3):403-11. PMID:17331072 doi:http://dx.doi.org/10.1042/BJ20061510
  6. ↑ Heckler EJ, Alon A, Fass D, Thorpe C. Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Biochemistry. 2008 Apr 29;47(17):4955-63. doi: 10.1021/bi702522q. Epub 2008 Apr, 5. PMID:18393449 doi:http://dx.doi.org/10.1021/bi702522q

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