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http://purl.uniprot.org/citations/25360546http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25360546http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25360546http://www.w3.org/2000/01/rdf-schema#comment"Apical membrane antigen 1 (AMA1) interacts with RON2 to form a protein complex that plays a key role in the invasion of host cells by malaria parasites. Blocking this protein-protein interaction represents a potential route to controlling malaria and related parasitic diseases, but the polymorphic nature of AMA1 has proven to be a major challenge to vaccine-induced antibodies and peptide inhibitors exerting strain-transcending inhibitory effects. Here we present the X-ray crystal structure of AMA1 domains I and II from Plasmodium falciparum strain FVO. We compare our new structure to those of AMA1 from P. falciparum 3D7 and Plasmodium vivax. A combination of normalized B factor analysis and computational methods has been used to investigate the flexibility of the domain I loops and how this correlates with their roles in determining the strain specificity of human antibody responses and inhibitory peptides. We also investigated the domain II loop, a key region involved in inhibitor binding, by comparison of multiple AMA1 crystal structures. Collectively, these results provide valuable insights that should contribute to the design of strain-transcending agents targeting P. falciparum AMA1."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.org/dc/terms/identifier"doi:10.1021/bi5012089"xsd:string
http://purl.uniprot.org/citations/25360546http://purl.org/dc/terms/identifier"doi:10.1021/bi5012089"xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Yang W."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Yang W."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Anders R.F."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Anders R.F."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"McGowan S."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"McGowan S."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Kannan Sivaraman K."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Kannan Sivaraman K."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Kass I."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Kass I."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Norton R.S."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Norton R.S."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Scammells P.J."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Scammells P.J."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Krishnarjuna B."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Krishnarjuna B."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"MacRaild C.A."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"MacRaild C.A."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Scanlon M.J."xsd:string
http://purl.uniprot.org/citations/25360546http://purl.uniprot.org/core/author"Scanlon M.J."xsd:string