2D68

Structure of the N-terminal domain of FOP (FGFR1OP) protein

Summary for 2D68

• Entry DOI: 10.2210/pdb2d68/pdb
• Descriptor: FOP (2 entities in total)
• Functional Keywords: alpha helical bundle, dimer, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, centrosome: O95684
• Total number of polymer chains: 2
• Total formula weight: 18309.01

Authors

Mikolajka, A. (deposition date: 2005-11-10, release date: 2006-05-16, Last modification date: 2024-03-13)

Primary citation

Mikolajka, A.,Yan, X.,Popowicz, G.M.,Smialowski, P.,Nigg, E.A.,Holak, T.A.
Structure of the N-terminal Domain of the FOP (FGFR1OP) Protein and Implications for its Dimerization and Centrosomal Localization.
J.Mol.Biol., 359:863-875, 2006

PubMed 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.

PubMed: 16690081
DOI: 10.1016/j.jmb.2006.03.070

Experimental method

X-RAY DIFFRACTION (1.6 Å)