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http://purl.uniprot.org/citations/16690081http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16690081http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16690081http://www.w3.org/2000/01/rdf-schema#comment"The fibroblast growth factor receptor 1 (FGFR1) oncogene partner, FOP, is a centrosomal protein that is involved in the anchoring of microtubules (MTS) to subcellular structures. The protein was originally discovered as a fusion partner with FGFR1 in oncoproteins that give rise to stem cell myeloproliferative disorders. A subsequent proteomics screen identified FOP as a component of the centrosome. FOP contains a Lis-homology (LisH) motif found in more than 100 eukaryotic proteins. LisH motifs are believed to be involved in microtubule dynamics and organization, cell migration, and chromosome segregation; several of them are associated with genetic diseases. We report here a 1.6A resolution crystal structure of the N-terminal dimerization domain of FOP. The structure comprises an alpha-helical bundle composed of two antiparallel chains, each of them having five alpha-helices. The central part of the dimer contains the LisH domain. We further determined that the FOP LisH domain is part of a longer N-terminal segment that is required, albeit not sufficient, for dimerization and centrosomal localization of FOP."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.03.070"xsd:string
http://purl.uniprot.org/citations/16690081http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.03.070"xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Nigg E.A."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Nigg E.A."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Yan X."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Yan X."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Holak T.A."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Holak T.A."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Popowicz G.M."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Popowicz G.M."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Mikolajka A."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Mikolajka A."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Smialowski P."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/author"Smialowski P."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/pages"863-875"xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/pages"863-875"xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/title"Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization."xsd:string
http://purl.uniprot.org/citations/16690081http://purl.uniprot.org/core/title"Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization."xsd:string