2d68

From Proteopedia

(Difference between revisions)

Revision as of 06:24, 30 May 2018

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

Structural highlights

2d68 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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

[FR1OP_HUMAN] Required for anchoring microtubules to the centrosomes.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yan X, Habedanck R, Nigg EA. A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring. Mol Biol Cell. 2006 Feb;17(2):634-44. Epub 2005 Nov 28. PMID:16314388 doi:E05-08-0810
↑ Mikolajka A, Yan X, Popowicz GM, Smialowski P, Nigg EA, Holak TA. Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization. J Mol Biol. 2006 Jun 16;359(4):863-75. Epub 2006 Apr 24. PMID:16690081 doi:S0022-2836(06)00474-8

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d68"

Categories: Human | Mikolajka, A | Alpha helical bundle | Cell cycle | Dimer

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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]] 1.60&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2d68]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
-</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://pdbe.org/2d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d68 RCSB], [http://www.ebi.ac.uk/pdbsum/2d68 PDBsum]</span></td></tr>
+</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://pdbe.org/2d68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d68 RCSB], [http://www.ebi.ac.uk/pdbsum/2d68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d68 ProSAT]</span></td></tr>
 </table>
 == Disease ==

2d68

From Proteopedia

Revision as of 06:24, 30 May 2018

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

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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