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Biophysical charact...
Biophysical characterization of the calmodulin-like domain of Plasmodium falciparum calcium dependent protein kinase 3
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- Andrésen, Cecilia (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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- Niklasson, Markus (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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- Cassman Eklöf, Sofie (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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- Wallner, Björn (author)
- Linköpings universitet,Bioinformatik,Tekniska fakulteten
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- Lundström, Patrik (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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(creator_code:org_t)
- 2017-07-26
- 2017
- English.
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In: PLOS ONE. - : PUBLIC LIBRARY SCIENCE. - 1932-6203. ; 12:7
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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