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==Oreochromis niloticus CEP120 second C2 domain (C2B) A200P + G307S mutant==
<StructureSection load='6ewi' size='340' side='right' caption='[[6ewi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ewi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nile_tilapia Nile tilapia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EWI FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cep120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8128 Nile tilapia])</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=6ewi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ewi OCA], [http://pdbe.org/6ewi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ewi RCSB], [http://www.ebi.ac.uk/pdbsum/6ewi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ewi ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Ciliopathies are a group of genetic disorders caused by a failure to form functional cilia. Due to a lack of structural information, it is currently poorly understood how ciliopathic mutations affect protein functionality to give rise to the underlying disease. Using X-ray crystallography, we show that the ciliopathy-associated centriolar protein CEP120 contains three C2 domains. The point mutations V194A and A199P, which cause Joubert syndrome (JS) and Jeune asphyxiating thoracic dystrophy (JATD), respectively, both reduce the thermostability of the second C2 domain by targeting residues that point toward its hydrophobic core. Genome-engineered cells homozygous for these mutations have largely normal centriole numbers but show reduced CEP120 levels, compromised recruitment of distal centriole markers, and deficient cilia formation. Our results provide insight into the disease mechanism of two ciliopathic mutations in CEP120, identify putative binding partners of CEP120 C2B, and suggest a complex genotype-phenotype relation of the CEP120 ciliopathy alleles.

Disease-Associated Mutations in CEP120 Destabilize the Protein and Impair Ciliogenesis.,Joseph N, Al-Jassar C, Johnson CM, Andreeva A, Barnabas DD, Freund SMV, Gergely F, van Breugel M Cell Rep. 2018 May 29;23(9):2805-2818. doi: 10.1016/j.celrep.2018.04.100. PMID:29847808<ref>PMID:29847808</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Nile tilapia]]
[[Category: Breugel, M van]]
[[Category: Centriole centrosome basal body cilia]]
[[Category: Cytosolic protein]]