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000472140 037__ $$aPUBDB-2021-04863
000472140 041__ $$aEnglish
000472140 1001_ $$0P:(DE-H253)PIP1080467$$aPazicky, Samuel$$b0
000472140 245__ $$aN-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum
000472140 260__ $$c2021
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000472140 520__ $$aAs the decline of malaria cases stalled over the last five years, novel targets in Plasmodium falciparum are necessary for the development of new drugs. Glycogen Synthase Kinase (PfGSK3) has been identified as a potential target, since its selective inhibitors were shown to disrupt the parasite’s life cycle. Here, we show that PfGSK3 exhibits autophosphorylation, leading to an extensive phosphorylation both in vitro and in the parasite. In the uncanonical N-terminal region of the parasite enzyme, we identified several autophosphorylation sites that regulate the activity of PfGSK3. By combining molecular modeling with experimental small-angle X-ray scattering data, we show that increased PfGSK3 activity is promoted by conformational changes in the PfGSK3 N-terminus, triggered by N-terminal phosphorylation. Our work provides novel insights into the structure and regulation of the malarial PfGSK3.
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000472140 7001_ $$aAlder, Arne$$b1
000472140 7001_ $$0P:(DE-H253)PIP1020991$$aMertens, Haydyn$$b2
000472140 7001_ $$0P:(DE-H253)PIP1001422$$aSvergun, Dmitri$$b3
000472140 7001_ $$aGilberger, Tim$$b4
000472140 7001_ $$0P:(DE-H253)PIP1030211$$aLoew, Christian$$b5$$eCorresponding author
000472140 773__ $$a10.1101/2021.06.18.448949
000472140 8564_ $$uhttps://www.biorxiv.org/content/10.1101/2021.06.18.448949v1
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