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Myeloperoxidase

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{{STRUCTURE_1myp| PDB=1myp | SIZE=400| SCENE= |right|CAPTION=Dog glycosylated myeloperoxidase dimer: heavy chain (pink and yellow), light chain (grey and green) containing heme complex with Ca+2 ions (green), [[1d5l]] }}
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<StructureSection load='1myp' size='350' side='right' caption='Dog glycosylated myeloperoxidase dimer: heavy chain (pink and yellow), light chain (grey and green) containing heme complex with Ca+2 ions (green) (PDB entry [[1myp]])' scene=''>
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== Function ==
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'''Myeloperoxidase''' (MPO) catalyzes the production of HOCl from hydrogen peroxide and chloride ion during the neutrophil respiratory burst. The hypochlorous acid is used by the neutrophil to kill bacteria and other pathogens<ref>PMID:10519157</ref>. MPO is a dimer consisting of 2 light chains and two variable-length heavy chains. MPO has a heme pigment which causes its green color in secretions like mucus which are rich in neutrophils.
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== Relevance ==
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MPO inhibitors are tested as therapeutic drugs in a number of kidney, inflammatory, cardiovascular, neurodegenerative and immune-mediated diseases<ref>PMID:11696548</ref>.
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'''Myeloperoxidase''' (MPO) catalyzes the production of HOCl from hydrogen peroxide and chloride ion during the neutrophil respiratory burst. The hypochlorous acid is used by the neutrophil to kill bacteria and other pathogens. MPO is a dimer consisting of 2 light chains and two variable-length heavy chains. MPO has a heme pigment which causes its green color in secretions like mucus which are rich in neutrophils.
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== Disease ==
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MPO is an important pathogenic factor in glomerular and tubulointestitial diseases<ref>PMID:14633118</ref>. MPO polymorphism is associated with increased risk of Alzheimer's disease<ref>PMID:26279325</ref>.
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</StructureSection>
==3D structures of myeloperoxidase==
==3D structures of myeloperoxidase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[1myp]] – MPO – dog<br />
 
[[1mhl]], [[1cxp]] – hMPO C – human<br />
[[1mhl]], [[1cxp]] – hMPO C – human<br />
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[[3f9p]] - hMPO<br />
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[[3f9p]], [[5fiw]], [[5mfa]], [[7oih]] - hMPO<br />
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[[1qo4]] - MPO – ''Arabidopsis thaliana''<br />
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[[1d2v]] – hMPO C + Br<br />
[[1d2v]] – hMPO C + Br<br />
[[1d5l]] – hMPO + CN<BR />
[[1d5l]] – hMPO + CN<BR />
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[[1dnu]] - hMPO + SCN<BR />
[[1dnu]] - hMPO + SCN<BR />
[[1dnw]] - hMPO + CN + SCN<BR />
[[1dnw]] - hMPO + CN + SCN<BR />
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[[3zs0]], [[3zs1]], [[4c1m]] - hMPO + inhibitor<br />
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[[3zs0]], [[3zs1]], [[4c1m]], [[5uzu]], [[5wdj]], [[5qj2]], [[5qj3]], [[6wxz]], [[6wy0]], [[6wy5]], [[6wy7]], [[6wyd]], [[7lae]], [[7lag]], [[7lal]], [[7lan]], [[7ni1]], [[7ni3]] - hMPO + inhibitor<br />
[[4dl1]] - hMPO + thioxanthine<br />
[[4dl1]] - hMPO + thioxanthine<br />
[[4ejx]] - hMPO + ceruplasmin<br />
[[4ejx]] - hMPO + ceruplasmin<br />
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[[6azp]], [[6bmt]], [[7qzr]], [[7z53]] - hMPO + staphylococcal peroxidase inhibitor<br />
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[[1myp]] – MPO – dog<br />
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[[1qo4]] - MPO – ''Arabidopsis thaliana''<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Dog glycosylated myeloperoxidase dimer: heavy chain (pink and yellow), light chain (grey and green) containing heme complex with Ca+2 ions (green) (PDB entry 1myp)

Drag the structure with the mouse to rotate

3D structures of myeloperoxidase

Updated on 10-July-2023

1mhl, 1cxp – hMPO C – human
3f9p, 5fiw, 5mfa, 7oih - hMPO
1d2v – hMPO C + Br
1d5l – hMPO + CN
1d7w - hMPO + CN + Br
1dnu - hMPO + SCN
1dnw - hMPO + CN + SCN
3zs0, 3zs1, 4c1m, 5uzu, 5wdj, 5qj2, 5qj3, 6wxz, 6wy0, 6wy5, 6wy7, 6wyd, 7lae, 7lag, 7lal, 7lan, 7ni1, 7ni3 - hMPO + inhibitor
4dl1 - hMPO + thioxanthine
4ejx - hMPO + ceruplasmin
6azp, 6bmt, 7qzr, 7z53 - hMPO + staphylococcal peroxidase inhibitor
1myp – MPO – dog
1qo4 - MPO – Arabidopsis thaliana

References

  1. ↑ Klebanoff SJ. Myeloperoxidase. Proc Assoc Am Physicians. 1999 Sep-Oct;111(5):383-9. PMID:10519157
  2. ↑ Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J Biol Chem. 2002 Jan 18;277(3):2160-8. Epub 2001 Nov 5. PMID:11696548 doi:10.1074/jbc.M109830200
  3. ↑ Malle E, Buch T, Grone HJ. Myeloperoxidase in kidney disease. Kidney Int. 2003 Dec;64(6):1956-67. PMID:14633118 doi:http://dx.doi.org/10.1046/j.1523-1755.2003.00336.x
  4. ↑ Lazarevic-Pasti T, Leskovac A, Vasic V. Myeloperoxidase Inhibitors as Potential Drugs. Curr Drug Metab. 2015;16(3):168-90. PMID:26279325

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