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Biophysical characterization of the calmodulin-like domain of Plasmodium falciparum calcium dependent protein kinase 3
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, Faculty of Science & Engineering.ORCID iD: 0000-0002-3772-8279
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2017 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 12, no 7, article id e0181721Article in journal (Refereed) Published
Abstract [en]

Calcium dependent protein kinases are unique to plants and certain parasites and comprise an N-terminal segment and a kinase domain that is regulated by a C-terminal calcium binding domain. Since the proteins are not found in man they are potential drug targets. We have characterized the calcium binding lobes of the regulatory domain of calcium dependent protein kinase 3 from the malaria parasite Plasmodium falciparum. Despite being structurally similar, the two lobes differ in several other regards. While the monomeric N-terminal lobe changes its structure in response to calcium binding and shows global dynamics on the sub-millisecond time-scale both in its apo and calcium bound states, the C-terminal lobe could not be prepared calcium-free and forms dimers in solution. If our results can be generalized to the full-length protein, they suggest that the C-terminal lobe is calcium bound even at basal levels and that activation is caused by the structural reorganization associated with binding of a single calcium ion to the N-terminal lobe.

Place, publisher, year, edition, pages
PUBLIC LIBRARY SCIENCE , 2017. Vol. 12, no 7, article id e0181721
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Structural Biology
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URN: urn:nbn:se:liu:diva-139916DOI: 10.1371/journal.pone.0181721ISI: 000406371800053PubMedID: 28746405OAI: oai:DiVA.org:liu-139916DiVA, id: diva2:1135443
Note

Funding Agencies|Vetenskapsradet [Dnr. 2012-5136, Dnr. 2012-5270]; Swedish e-science

Available from: 2017-08-23 Created: 2017-08-23 Last updated: 2018-03-27

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