Journal Article

PUBDB-2022-01747

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png N-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum

Pazicky, S.CSSB* ; Alder, A. ; Mertens, H. ; Svergun, D. ; Gilberger, T. ; Loew, C. (Corresponding author)CSSB*

2022
Portland Pr. London [u.a.]

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Please use a persistent id in citations: doi:10.1042/BCJ20210829  doi:10.3204/PUBDB-2022-01747

Abstract: As 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 parasitès life cycle. In the uncanonical N-terminal region of the parasite enzyme, we identified several autophosphorylation sites and probed their role in activity regulation 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.

Note: ISSN 1470-8728 not unique: **2 hits**.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)
2. EMBL (EMBL)
3. CSSB-EMBL (CSSB-EMBL)
4. CSSB-EMBL-CL (CSSB-EMBL-CL)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2022

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Database coverage:
; ; ; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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