Combining IP₃ affinity chromatography and bioinformatics reveals a novel protein-IP₃ binding site on Plasmodium falciparum MDR1 transporter.

ABSTRACT: Intracellular Ca²⁺ mobilization induced by second messenger IP₃ controls many cellular events in most of the eukaryotic groups. Despite the increasing evidence of IP₃-induced Ca²⁺ in apicomplexan parasites like Plasmodium, responsible for malaria infection, no protein with potential function as an IP₃-receptor has been identified. The use of bioinformatic analyses based on previously known sequences of IP₃-receptor failed to identify potential IP₃-receptor candidates in any Apicomplexa. In this work, we combine the biochemical approach of an IP₃ affinity chromatography column with bioinformatic meta-analyses to identify potential vital membrane proteins that present binding with IP_3</

SUBMITTER: Alves E 

PROVIDER: S-EPMC9792294 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature