2d68
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(New page: 200px<br /> <applet load="2d68" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d68, resolution 1.60Å" /> '''Structure of the N-...)
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Revision as of 19:20, 12 November 2007
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Structure of the N-terminal domain of FOP (FGFR1OP) protein
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Fibrodysplasia ossificans progressiva OMIM:[102576], Myeloproliferative disorder OMIM:[605392]
About this Structure
2D68 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization., Mikolajka A, Yan X, Popowicz GM, Smialowski P, Nigg EA, Holak TA, J Mol Biol. 2006 Jun 16;359(4):863-75. Epub 2006 Apr 24. PMID:16690081
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