{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Le Berre M"],"funding":["National Institute of Allergy and Infectious Diseases","Vetenskapsrådet","French Infrastructure for Integrated Structural Biology","NIAID NIH HHS","Université Paris-Saclay, Ecoles doctorales, Université Paris-Saclay","CNRS ATIP-Avenir","Grand Équipement National De Calcul Intensif","ANRS-MIE","Ministère de l'Education Nationale, de l'Enseignement Superieur et de la Recherche"],"pagination":["38-48"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11740583"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["81(Pt 1)"],"pubmed_abstract":["The apicomplexan AP2 (ApiAP2) proteins are the best characterized family of DNA-binding proteins in Plasmodium spp. malaria parasites. Apart from the AP2 DNA-binding domain, there is little sequence similarity between ApiAP2 proteins. However, a conserved AP2-coincident domain mostly at the C-terminus (ACDC domain) is observed in a subset of the ApiAP2 proteins. The structure and function of this domain remain unknown. We report two crystal structures of ACDC domains derived from distinct Plasmodium ApiAP2 proteins, revealing a conserved, unique, noncanonical, four-helix bundle architecture. We used these structures to perform in silico docking calculations against a library of known antimalarial compounds and identified potential small-molecule ligands that bind in a highly conserved hydr"],"journal":["Acta crystallographica. Section D, Structural biology"],"pubmed_title":["Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites."],"pmcid":["PMC11740583"],"funding_grant_id":["ECTZ189696","R01AI125565","AD010714400","ANR-10-INSB-05-05","R01 AI125565"],"pubmed_authors":["Lazar N","Li de la Sierra-Gallay I","Tubiana T","Llinas M","Reutersward Waldner P","Santos JM","Le Berre M","Nessler S"],"additional_accession":[]},"is_claimable":false,"name":"Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites.","description":"The apicomplexan AP2 (ApiAP2) proteins are the best characterized family of DNA-binding proteins in Plasmodium spp. malaria parasites. Apart from the AP2 DNA-binding domain, there is little sequence similarity between ApiAP2 proteins. However, a conserved AP2-coincident domain mostly at the C-terminus (ACDC domain) is observed in a subset of the ApiAP2 proteins. The structure and function of this domain remain unknown. We report two crystal structures of ACDC domains derived from distinct Plasmodium ApiAP2 proteins, revealing a conserved, unique, noncanonical, four-helix bundle architecture. We used these structures to perform in silico docking calculations against a library of known antimalarial compounds and identified potential small-molecule ligands that bind in a highly conserved hydr","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-07-15T13:51:54.585Z","creation":"2026-07-05T03:11:30.655Z"},"accession":"S-EPMC11740583","cross_references":{"pubmed":["39820027"],"doi":["10.1107/S2059798324012518","10.1107/s2059798324012518"]}}