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http://purl.uniprot.org/citations/34316015http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34316015http://www.w3.org/2000/01/rdf-schema#comment"Apolipoprotein L1 (ApoL1) is a circulating innate immunity protein protecting against trypanosome infection. However, two ApoL1 coding variants are associated with a highly increased risk of chronic kidney disease. Here we present X-ray and NMR structures of the N-terminal domain (NTD) of ApoL1 and of its closest relative ApoL2. In both proteins, four of the five NTD helices form a four-helix core structure which is different from the classical four-helix bundle and from the pore-forming domain of colicin A. The reactivity with a conformation-specific antibody and structural models predict that this four-helix motif is also present in the NTDs of ApoL3 and ApoL4, suggesting related functions within the small ApoL family. The long helix 5 of ApoL1 is conformationally flexible and contains the BH3-like region. This BH3-like α-helix resembles true BH3 domains only in sequence and structure but not in function, since it does not bind to the pro-survival members of the Bcl-2 family, suggesting a Bcl-2-independent role in cytotoxicity. These findings should expedite a more comprehensive structural and functional understanding of the ApoL immune protein family."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.org/dc/terms/identifier"doi:10.1038/s42003-021-02387-5"xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Moran P."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Gupta N."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Eigenbrot C."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Chiu C."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Scales S.J."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Ultsch M."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Holliday M.J."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Fairbrother W."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Kirchhofer D."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Gerhardy S."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/author"Oltrabella F."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/name"Commun Biol"xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/pages"916"xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/title"Structures of the ApoL1 and ApoL2 N-terminal domains reveal a non-classical four-helix bundle motif."xsd:string
http://purl.uniprot.org/citations/34316015http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/34316015http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34316015
http://purl.uniprot.org/citations/34316015http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34316015
http://purl.uniprot.org/uniprot/#_B4E1T5-mappedCitation-34316015http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34316015
http://purl.uniprot.org/uniprot/#_O14791-mappedCitation-34316015http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34316015
http://purl.uniprot.org/uniprot/#_Q9BQE5-mappedCitation-34316015http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34316015
http://purl.uniprot.org/uniprot/O14791http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34316015