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http://purl.uniprot.org/citations/15713464http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15713464http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15713464http://www.w3.org/2000/01/rdf-schema#comment"Human hookworm infection is a major cause of anemia and malnutrition of adults and children in the developing world. As part of on-going efforts to control hookworm infection, The Human Hookworm Vaccine Initiative has identified candidate vaccine antigens from the infective L3 larval stages of the parasite, including a family of pathogenesis-related (PR) proteins known as the Ancylostoma-secreted proteins (ASPs). A novel crystal structure of Na-ASP-2, a PR-1 protein secreted by infective larvae of the human hookworm Necator americanus, has been solved to resolution limits of 1.68 A and to an R-factor of 17% using the recombinant protein expressed in and secreted by Pichia pastoris. The overall fold of Na-ASP-2 is a three-layer alphabetaalpha sandwich flanked by an N-terminal loop and a short, cysteine-rich C terminus. Our structure reveals a large central cavity that is flanked by His129 and Glu106, two residues that are well conserved in all parasitic nematode L3 ASPs. Na-ASP-2 has structural and charge similarities to chemokines, which suggests that Na-ASP-2 may be an extra-cellular ligand of an unknown receptor. Na-ASP-2 is a useful homology model for NIF, a natural antagonistic ligand of CR3 receptor. From these modeling studies, possible binding modes were predicted. In addition, this first structure of a PR-1 protein from parasitic helminths may shed light on the molecular basis of host-parasite interactions."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2004.12.023"xsd:string
http://purl.uniprot.org/citations/15713464http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2004.12.023"xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Asojo O.A."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Asojo O.A."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Hotez P.J."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Hotez P.J."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Loukas A."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Loukas A."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Zhan B."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Zhan B."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Dhar K."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Dhar K."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Borgstahl G.E."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Borgstahl G.E."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Deumic V."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Deumic V."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Goud G."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/author"Goud G."xsd:string
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15713464http://purl.uniprot.org/core/date"2005"xsd:gYear