Plasmepsin: Difference between revisions
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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)'''. | |||
*'''Proplasmepsin II''' exhibits a large shift between its domains which renders the protease inactive. | |||
==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 /> | ||
*Plasmepsin IV | |||
**[[2anl]] – Plm IV + statine derivative – ''Plasmodium malariae''<br /> | |||
**[[1ls5]] - PfPlm IV + pepstatin derivative<br /> | |||
*Proplasmepsin II | *Proplasmepsin II | ||
| Line 34: | Line 45: | ||
**[[1miq]] – PvProPlm II – ''Plasmodium vivax''<br /> | **[[1miq]] – PvProPlm II – ''Plasmodium vivax''<br /> | ||
**[[1qs8]] - PvPlm + pepstatin derivative<br /> | **[[1qs8]] - PvPlm + pepstatin derivative<br /> | ||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:50, 4 July 2016
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
- ↑ 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:https://dx.doi.org/10.1021/jm5014133
References
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Michal Harel, Joel L. Sussman, Jaime Prilusky
