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2d68

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Revision as of 18:42, 20 September 2023

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

Structural highlights

2d68 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

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).^[1]

Function

CEP43_HUMAN Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385).^[2] ^[3] ^[4]

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^[5]

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

References

↑ Popovici C, Zhang B, Grégoire MJ, Jonveaux P, Lafage-Pochitaloff M, Birnbaum D, Pébusque MJ. The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1. Blood. 1999 Feb 15;93(4):1381-9 PMID:9949182
↑ 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
↑ Kanie T, Abbott KL, Mooney NA, Plowey ED, Demeter J, Jackson PK. The CEP19-RABL2 GTPase Complex Binds IFT-B to Initiate Intraflagellar Transport at the Ciliary Base. Dev Cell. 2017 Jul 10;42(1):22-36.e12. PMID:28625565 doi:10.1016/j.devcel.2017.05.016
↑ Mojarad BA, Gupta GD, Hasegan M, Goudiam O, Basto R, Gingras AC, Pelletier L. CEP19 cooperates with FOP and CEP350 to drive early steps in the ciliogenesis programme. Open Biol. 2017 Jun;7(6):170114. PMID:28659385 doi:10.1098/rsob.170114
↑ 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: Homo sapiens | Large Structures | Mikolajka A

@@ Line 3: / Line 3: @@
 <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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2D68 FirstGlance]. <br>
+<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>
-</td></tr><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>
+</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>
+<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>
 </table>
 == Disease ==
-[[https://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.
+[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>
 == Function ==
-[[https://www.uniprot.org/uniprot/FR1OP_HUMAN FR1OP_HUMAN]] Required for anchoring microtubules to the centrosomes.<ref>PMID:16314388</ref>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Mikolajka, A]]
+[[Category: Mikolajka A]]
-[[Category: Alpha helical bundle]]
-[[Category: Cell cycle]]
-[[Category: Dimer]]

2d68

From Proteopedia

Revision as of 18:42, 20 September 2023

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?)

Views

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