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5lph

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Structure of the TOG domain of human Cep104

Structural highlights

5lph 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 2.25Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CE104_HUMAN The disease is caused by mutations affecting the gene represented in this entry.

Function

CE104_HUMAN Required for ciliogenesis and for structural integrity at the ciliary tip.^[1]

Publication Abstract from PubMed

Cilia are thin cell projections with essential roles in cell motility, fluid movement, sensing, and signaling. They are templated from centrioles that dock against the plasma membrane and subsequently extend their peripheral microtubule array. The molecular mechanisms underpinning cilia assembly are incompletely understood. Cep104 is a key factor involved in cilia formation and length regulation that rides on the ends of elongating and shrinking cilia. It is mutated in Joubert syndrome, a genetically heterogeneous ciliopathy. Here we provide structural and biochemical data that Cep104 contains a tubulin-binding TOG (tumor overexpressed gene) domain and a novel C2HC zinc finger array. Furthermore, we identify the kinase Nek1, another ciliopathy-associated protein, as a potential binding partner of this array. Finally, we show that Nek1 competes for binding to Cep104 with the distal centriole-capping protein CP110. Our data suggest a model for Cep104 activity during ciliogenesis and provide a novel link between Cep104 and Nek1.

The Ciliopathy-Associated Cep104 Protein Interacts with Tubulin and Nek1 Kinase.,Al-Jassar C, Andreeva A, Barnabas DD, McLaughlin SH, Johnson CM, Yu M, van Breugel M Structure. 2017 Jan 3;25(1):146-156. doi: 10.1016/j.str.2016.11.014. Epub 2016, Dec 22. PMID:28017521^[2]

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

References

↑ Satish Tammana TV, Tammana D, Diener DR, Rosenbaum J. Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the ciliary tip during ciliary assembly. J Cell Sci. 2013 Nov 1;126(Pt 21):5018-29. doi: 10.1242/jcs.133439. Epub 2013 Aug, 22. PMID:23970417 doi:http://dx.doi.org/10.1242/jcs.133439
↑ Al-Jassar C, Andreeva A, Barnabas DD, McLaughlin SH, Johnson CM, Yu M, van Breugel M. The Ciliopathy-Associated Cep104 Protein Interacts with Tubulin and Nek1 Kinase. Structure. 2017 Jan 3;25(1):146-156. doi: 10.1016/j.str.2016.11.014. Epub 2016, Dec 22. PMID:28017521 doi:http://dx.doi.org/10.1016/j.str.2016.11.014

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/5lph"

Categories: Homo sapiens | Large Structures | Van Breugel M

@@ Line 3: / Line 3: @@
 <StructureSection load='5lph' size='340' side='right'caption='[[5lph]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lph]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LPH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LPH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lph]] 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=5LPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LPH FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.25&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lph OCA], [http://pdbe.org/5lph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lph RCSB], [http://www.ebi.ac.uk/pdbsum/5lph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lph ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5lph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lph OCA], [https://pdbe.org/5lph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lph RCSB], [https://www.ebi.ac.uk/pdbsum/5lph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lph ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CE104_HUMAN CE104_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/CE104_HUMAN CE104_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/CE104_HUMAN CE104_HUMAN]] Required for ciliogenesis and for structural integrity at the ciliary tip.<ref>PMID:23970417</ref>
+[https://www.uniprot.org/uniprot/CE104_HUMAN CE104_HUMAN] Required for ciliogenesis and for structural integrity at the ciliary tip.<ref>PMID:23970417</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Breugel, M van]]
+[[Category: Van Breugel M]]
-[[Category: Basal body]]
-[[Category: Cell cycle]]
-[[Category: Centriole]]
-[[Category: Cep104]]
-[[Category: Cilia]]
-[[Category: Heat repeat]]
-[[Category: Tog domain]]
-[[Category: Tubulin binding]]

5lph

From Proteopedia

Current revision

Structure of the TOG domain of human Cep104

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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