3f9p

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[[Image:3f9p.png|left|200px]]
 
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{{STRUCTURE_3f9p| PDB=3f9p | SCENE= }}
{{STRUCTURE_3f9p| PDB=3f9p | SCENE= }}
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===Crystal structure of myeloperoxidase from human leukocytes===
===Crystal structure of myeloperoxidase from human leukocytes===
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{{ABSTRACT_PUBMED_19608745}}
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{{ABSTRACT_PUBMED_19608745}}
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==Disease==
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[[http://www.uniprot.org/uniprot/PERM_HUMAN PERM_HUMAN]] Defects in MPO are the cause of myeloperoxidase deficiency (MPOD) [MIM:[http://omim.org/entry/254600 254600]]. A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis.<ref>PMID:8142659</ref><ref>PMID:7904599</ref><ref>PMID:8621627</ref><ref>PMID:9637725</ref><ref>PMID:9354683</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/PERM_HUMAN PERM_HUMAN]] Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:019608745</ref><references group="xtra"/>
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<ref group="xtra">PMID:019608745</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]

Revision as of 21:48, 24 March 2013

Template:STRUCTURE 3f9p

Contents

Crystal structure of myeloperoxidase from human leukocytes

Template:ABSTRACT PUBMED 19608745

Disease

[PERM_HUMAN] Defects in MPO are the cause of myeloperoxidase deficiency (MPOD) [MIM:254600]. A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis.[1][2][3][4][5]

Function

[PERM_HUMAN] Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.

About this Structure

3f9p is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Carpena X, Vidossich P, Schroettner K, Calisto BM, Banerjee S, Stampler J, Soudi M, Furtmuller PG, Rovira C, Fita I, Obinger C. Essential role of proximal histidine-asparagine interaction in mammalian peroxidases. J Biol Chem. 2009 Sep 18;284(38):25929-37. Epub 2009 Jul 16. PMID:19608745 doi:10.1074/jbc.M109.002154
  1. ↑ Kizaki M, Miller CW, Selsted ME, Koeffler HP. Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency. Blood. 1994 Apr 1;83(7):1935-40. PMID:8142659
  2. ↑ Nauseef WM, Brigham S, Cogley M. Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan. J Biol Chem. 1994 Jan 14;269(2):1212-6. PMID:7904599
  3. ↑ Nauseef WM, Cogley M, McCormick S. Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem. 1996 Apr 19;271(16):9546-9. PMID:8621627
  4. ↑ DeLeo FR, Goedken M, McCormick SJ, Nauseef WM. A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J Clin Invest. 1998 Jun 15;101(12):2900-9. PMID:9637725 doi:10.1172/JCI2649
  5. ↑ Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE. Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood. 1997 Nov 15;90(10):4126-34. PMID:9354683

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