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2d68
From Proteopedia
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| - | + | ==Structure of the N-terminal domain of FOP (FGFR1OP) protein== | |
| - | + | <StructureSection load='2d68' size='340' side='right' caption='[[2d68]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2d68]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D68 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2d68 RCSB], [http://www.ebi.ac.uk/pdbsum/2d68 PDBsum]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/FR1OP_HUMAN FR1OP_HUMAN]] Note=A chromosomal aberration involving FGFR1OP 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 FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity. | [[http://www.uniprot.org/uniprot/FR1OP_HUMAN FR1OP_HUMAN]] Note=A chromosomal aberration involving FGFR1OP 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 FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FR1OP_HUMAN FR1OP_HUMAN]] Required for anchoring microtubules to the centrosomes.<ref>PMID:16314388</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:16690081</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Mikolajka, A | + | [[Category: Mikolajka, A]] |
[[Category: Alpha helical bundle]] | [[Category: Alpha helical bundle]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Dimer]] | [[Category: Dimer]] | ||
Revision as of 12:01, 18 December 2014
Structure of the N-terminal domain of FOP (FGFR1OP) protein
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