2d68

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[[Image:2d68.gif|left|200px]]
 
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==Structure of the N-terminal domain of FOP (FGFR1OP) protein==
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The line below this paragraph, containing "STRUCTURE_2d68", creates the "Structure Box" on the page.
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<StructureSection load='2d68' size='340' side='right'caption='[[2d68]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2d68]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D68 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d68 OCA], [https://pdbe.org/2d68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d68 RCSB], [https://www.ebi.ac.uk/pdbsum/2d68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d68 ProSAT]</span></td></tr>
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{{STRUCTURE_2d68| PDB=2d68 | SCENE= }}
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</table>
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== Disease ==
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'''Structure of the N-terminal domain of FOP (FGFR1OP) protein'''
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[https://www.uniprot.org/uniprot/CEP43_HUMAN CEP43_HUMAN] A chromosomal aberration involving CEP43 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion proteins CEP43-FGFR1 or FGFR1-CEP43 may exhibit constitutive kinase activity and be responsible for the transforming activity (PubMed:9949182).<ref>PMID:9949182</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CEP43_HUMAN CEP43_HUMAN] Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385).<ref>PMID:16314388</ref> <ref>PMID:28625565</ref> <ref>PMID:28659385</ref>
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==Overview==
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== References ==
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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.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2D68 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D68 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16690081 16690081]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Mikolajka, A.]]
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[[Category: Mikolajka A]]
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[[Category: Alpha helical bundle]]
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[[Category: Dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:46:43 2008''
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Current revision

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

PDB ID 2d68

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