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- W2000499546 abstract "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 1.6 Å resolution crystal structure of the N-terminal dimerization domain of FOP. The structure comprises an α-helical bundle composed of two antiparallel chains, each of them having five α-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." @default.
- W2000499546 created "2016-06-24" @default.
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- W2000499546 date "2006-06-01" @default.
- W2000499546 modified "2023-09-23" @default.
- W2000499546 title "Structure of the N-terminal Domain of the FOP (FGFR1OP) Protein and Implications for its Dimerization and Centrosomal Localization" @default.
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- W2000499546 doi "https://doi.org/10.1016/j.jmb.2006.03.070" @default.
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