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http://purl.uniprot.org/citations/24497644http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24497644http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24497644http://www.w3.org/2000/01/rdf-schema#comment"Atherosclerosis is associated with chronic inflammation occurring over decades. The enzyme 15-lipoxygenase-2 (15-LOX-2) is highly expressed in large atherosclerotic plaques, and its activity has been linked to the progression of macrophages to the lipid-laden foam cells present in atherosclerotic plaques. We report here the crystal structure of human 15-LOX-2 in complex with an inhibitor that appears to bind as a substrate mimic. 15-LOX-2 contains a long loop, composed of hydrophobic amino acids, which projects from the amino-terminal membrane-binding domain. The loop is flanked by two Ca(2+)-binding sites that confer Ca(2+)-dependent membrane binding. A comparison of the human 15-LOX-2 and 5-LOX structures reveals similarities at the active sites, as well striking differences that can be exploited for design of isoform-selective inhibitors."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.543777"xsd:string
http://purl.uniprot.org/citations/24497644http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.543777"xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Neau D.B."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Neau D.B."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Newcomer M.E."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Newcomer M.E."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Bartlett S.G."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Bartlett S.G."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Kobe M.J."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Kobe M.J."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Mitchell C.E."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/author"Mitchell C.E."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/pages"8562-8569"xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/pages"8562-8569"xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/title"The structure of human 15-lipoxygenase-2 with a substrate mimic."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/title"The structure of human 15-lipoxygenase-2 with a substrate mimic."xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/volume"289"xsd:string
http://purl.uniprot.org/citations/24497644http://purl.uniprot.org/core/volume"289"xsd:string