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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'''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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== 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 ==
== References ==
<references/>
<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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