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Publikācija: Crystal Structure of Plasmodium Falciparum Proplasmepsin IV: The Plasticity of Proplasmepsins

Publication Type Scientific article indexed in SCOPUS or WOS database
Funding for basic activity Unknown
Defending: ,
Publication language English (en)
Title in original language Crystal Structure of Plasmodium Falciparum Proplasmepsin IV: The Plasticity of Proplasmepsins
Field of research 1. Natural sciences
Sub-field of research 1.4 Chemical sciences
Authors R. Recacha
Kristaps Jaudzems
I. Akopjana
Aigars Jirgensons
K. Tars
Keywords aspartic protease zymogen | malaria | Plasmodium falciparum | proplasmepsin IV
Abstract 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 Å 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.
DOI: 10.1107/S2053230X16011663
Hyperlink: http://scripts.iucr.org/cgi-bin/paper?S2053230X16011663 
Reference Recacha, R., Jaudzems, K., Akopjana, I., Jirgensons, A., Tars, K. Crystal Structure of Plasmodium Falciparum Proplasmepsin IV: The Plasticity of Proplasmepsins. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2016, Vol.72, pp.659-666. ISSN 2053-230X. Available from: doi:10.1107/S2053230X16011663
Additional information Citation count:
ID 23185