Plasmepsin
From Proteopedia
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{{STRUCTURE_3fns| right| PDB=3fns | SCENE= |CAPTION=Plasmepsin dimer witn Zn+2 ions (grey), [[3fns]] }} | {{STRUCTURE_3fns| right| PDB=3fns | SCENE= |CAPTION=Plasmepsin dimer witn Zn+2 ions (grey), [[3fns]] }} | ||
| - | [[Plasmepsin]] (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite | + | == Function == |
| + | [[Plasmepsin]] (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite. It is an aspartic acid protease having 2 aspartic acid residues in the active site. Ten Plm isoforms are known which are named Plm I, II, etc and '''Histo-Aspartic Protease (HAP)'''. | ||
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| + | *'''Proplasmepsin II''' exhibits a large shift between its domains which renders the protease inactive. | ||
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| + | ==Relevance == | ||
| + | Plm is a potential target for anti-malaria drugs<ref>PMID:25719272</ref>. | ||
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**[[1w6i]], [[1xdh]], [[1xe5]], [[1xe6]], [[1me6]], [[1sme]] – PfPlm II + pepstatin derivative<br /> | **[[1w6i]], [[1xdh]], [[1xe5]], [[1xe6]], [[1me6]], [[1sme]] – PfPlm II + pepstatin derivative<br /> | ||
**[[1m43]] - PfPlm II (mutant) + pepstatin derivative<br /> | **[[1m43]] - PfPlm II (mutant) + pepstatin derivative<br /> | ||
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| + | *Plasmepsin IV | ||
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| + | **[[2anl]] – Plm IV + statine derivative – ''Plasmodium malariae''<br /> | ||
| + | **[[1ls5]] - PfPlm IV + pepstatin derivative<br /> | ||
*Proplasmepsin II | *Proplasmepsin II | ||
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**[[1miq]] – PvProPlm II – ''Plasmodium vivax''<br /> | **[[1miq]] – PvProPlm II – ''Plasmodium vivax''<br /> | ||
**[[1qs8]] - PvPlm + pepstatin derivative<br /> | **[[1qs8]] - PvPlm + pepstatin derivative<br /> | ||
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| - | *Plasmepsin IV | ||
| - | |||
| - | **[[2anl]] – Plm IV + statine derivative – ''Plasmodium malariae''<br /> | ||
| - | **[[1ls5]] - PfPlm IV + pepstatin derivative<br /> | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:50, 4 July 2016
Contents |
Function
Plasmepsin (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite. It is an aspartic acid protease having 2 aspartic acid residues in the active site. Ten Plm isoforms are known which are named Plm I, II, etc and Histo-Aspartic Protease (HAP).
- Proplasmepsin II exhibits a large shift between its domains which renders the protease inactive.
Relevance
Plm is a potential target for anti-malaria drugs[1].
3D structures of plasmepsin
Updated on 04-July-2016
References
- ↑ Huizing AP, Mondal M, Hirsch AK. Fighting malaria: structure-guided discovery of nonpeptidomimetic plasmepsin inhibitors. J Med Chem. 2015 Jul 9;58(13):5151-63. doi: 10.1021/jm5014133. Epub 2015 Mar 17. PMID:25719272 doi:http://dx.doi.org/10.1021/jm5014133
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Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
