Structural highlights
Publication Abstract from PubMed
Plasmepsin IV from Plasmodium falciparum (PM IV) is a promising target for the development of novel antimalarial drugs. Here, the crystal structure of the truncated zymogen of PM IV (pPM IV), consisting of the mature enzyme plus a prosegment of 47 residues, has been determined at 1.5 A resolution. pPM IV presents the fold previously described for studied proplasmepsins, displaying closer similarities to proplasmepin IV from P. vivax (pPvPM) than to the other two proplasmepsins from P. falciparum. The study and comparison of the pPM IV structure with the proplasmepsin structures described previously provide information about the similarities and differences in the inactivation-activation mechanisms among the plasmepsin zymogens.
Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins.,Recacha R, Jaudzems K, Akopjana I, Jirgensons A, Tars K Acta Crystallogr F Struct Biol Commun. 2016 Sep;72(Pt 9):659-66. doi:, 10.1107/S2053230X16011663. Epub 2016 Aug 9. PMID:27599854[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Recacha R, Jaudzems K, Akopjana I, Jirgensons A, Tars K. Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins. Acta Crystallogr F Struct Biol Commun. 2016 Sep;72(Pt 9):659-66. doi:, 10.1107/S2053230X16011663. Epub 2016 Aug 9. PMID:27599854 doi:http://dx.doi.org/10.1107/S2053230X16011663