A comparative study between the datasets of AlphaFold 3 generated 3D structures of Leishmania and Trypanosoma AMPKα, the catalytic subunit
Description
Leishmania is a human protozoan parasite that causes leishmaniasis in tropical and sub-tropical regions. It displays a complex life cycle, alternating between sandfly vectors and mammalian hosts, where it encounters diverse environmental and metabolic stresses. AMP-activated protein kinase (AMPK) is an evolutionarily conserved serine/threonine kinase that regulates energy homeostasis and cellular metabolism in eukaryotes by sensing nutrient and oxygen supply in the ambience. AMPK has been shown to be involved in nutrient sensing, stress response and proliferation in Trypanosoma. Leishmania and Trypanosoma, both belong to the family Trypanosomatidae are evolutionary closely related. However, it was poorly characterized in Leishmania. AMPK is a heterotrimeric complex consisting of one catalytic α subunit and two regulatory subunits (β and γ). We identified and annotated clinically relevant orthologous Leishmania AMPK (LAMPK) protein subunit sequences from TritrypDB. Furthermore, since there were no tertiary structures available in database, we have generated these structures of Leishmania and Trypanosoma AMPKα using AlphaFold3. Determination of important parameters such as pLDDT, pTM scores indicate ‘true’ structures. Sequence and structure analyses revealed similarities and differences between Leishmania and Trypnosoma AMPKα proteins.
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Institutions
- University of Calcutta Department of Biochemistry