Plasmepsin

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	**[[1ls5]] - PfPlm IV + pepstatin derivative<br />		**[[1ls5]] - PfPlm IV + pepstatin derivative<br />
-	*Plasmepsin V	+	*Plasmepsin V or aspartic protease PM5
	**[[6c4g]] – PvPlm V + inhibitor<br />		**[[6c4g]] – PvPlm V + inhibitor<br />
		+
		+	*Plasmepsin X
		+
		+	**[[6ors]] – PvPlm X <br />
	*Proplasmepsin II		*Proplasmepsin II

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Revision as of 10:42, 12 January 2022

spinqualitylabelsall models Plasmepsin II complex with a potential antimalarial drug (PDB entry 4cku) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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[1]. Relevance Plm is a potential target for anti-malaria drugs[2]. Structural highlights The active site of Plm II contains a [3]. . Water molecules are shown as red spheres.

3D structures of plasmepsin

Updated on 12-January-2022

References

1. ↑ Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN. Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum. Nat Struct Biol. 1999 Jan;6(1):32-7. PMID:9886289 doi:10.1038/4905
2. ↑ 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
3. ↑ Jaudzems K, Tars K, Maurops G, Ivdra N, Otikovs M, Leitans J, Kanepe-Lapsa I, Domraceva I, Mutule I, Trapencieris P, Blackman MJ, Jirgensons A. Plasmepsin inhibitory activity and structure-guided optimization of a potent hydroxyethylamine-based antimalarial hit. ACS Med Chem Lett. 2014 Jan 13;5(4):373-7. doi: 10.1021/ml4004952. eCollection, 2014 Apr 10. PMID:24900843 doi:http://dx.doi.org/10.1021/ml4004952