| Literature DB >> 16690081 |
Aleksandra Mikolajka1, Xiumin Yan, Grzegorz M Popowicz, Pawel Smialowski, Erich A Nigg, Tad A Holak.
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 1.6A 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.Entities:
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Year: 2006 PMID： 16690081 DOI： 10.1016/j.jmb.2006.03.070
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469