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| | ==Human CEP135 parallel dimeric coiled coil 82-144== | | ==Human CEP135 parallel dimeric coiled coil 82-144== |
| - | <StructureSection load='5ng4' size='340' side='right' caption='[[5ng4]], [[Resolution|resolution]] 2.14Å' scene=''> | + | <StructureSection load='5ng4' size='340' side='right'caption='[[5ng4]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ng4]] 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=5NG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NG4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ng4]] 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=5NG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NG4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CEP135, CEP4, KIAA0635 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.14Å</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=5ng4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ng4 OCA], [http://pdbe.org/5ng4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ng4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ng4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ng4 ProSAT]</span></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=5ng4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ng4 OCA], [https://pdbe.org/5ng4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ng4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ng4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ng4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CP135_HUMAN CP135_HUMAN]] Autosomal recessive primary microcephaly. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/CP135_HUMAN CP135_HUMAN] Autosomal recessive primary microcephaly. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CP135_HUMAN CP135_HUMAN]] Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole.<ref>PMID:17681131</ref> <ref>PMID:18851962</ref> <ref>PMID:26675238</ref> | + | [https://www.uniprot.org/uniprot/CP135_HUMAN CP135_HUMAN] Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole.<ref>PMID:17681131</ref> <ref>PMID:18851962</ref> <ref>PMID:26675238</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Bianchi, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Kraatz, S H.W]] | + | [[Category: Bianchi S]] |
| - | [[Category: Steinmetz, M O]] | + | [[Category: Kraatz SHW]] |
| - | [[Category: Centrosome]] | + | [[Category: Steinmetz MO]] |
| - | [[Category: Cep135]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Disulfide bridge]]
| + | |
| - | [[Category: Microtubule-binding protein]]
| + | |
| Structural highlights
Disease
CP135_HUMAN Autosomal recessive primary microcephaly. The disease is caused by mutations affecting the gene represented in this entry.
Function
CP135_HUMAN Centrosomal protein involved in centriole biogenesis. Acts as a scaffolding protein during early centriole biogenesis. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also required for centriole-centriole cohesion during interphase by acting as a platform protein for CEP250 at the centriole.[1] [2] [3]
Publication Abstract from PubMed
Coiled coils are ubiquitous protein-protein interaction motifs found in many eukaryotic proteins. The elongated, flexible and often irregular natureof coiled coils together with their tendency to form fibrous arrangements in crystals impose challenges on solving the phase problem by molecular replacement. Here, we report the successful combinatorial use of native- and rational engineered disulfide bridges together with sulfur-SAD phasing as a powerful tool to stabilize and solve the structure of coiled-coil domains in a straightforward manner. Our study is a key example of how modern sulfur SAD combined with mutagenesis can help to advance and simplify the structural study of challenging coiled-coil domains by X-ray crystallography.
Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils.,Kraatz SHW, Bianchi S, Steinmetz MO Biosci Rep. 2018 Aug 22. pii: BSR20181073. doi: 10.1042/BSR20181073. PMID:30135143[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kleylein-Sohn J, Westendorf J, Le Clech M, Habedanck R, Stierhof YD, Nigg EA. Plk4-induced centriole biogenesis in human cells. Dev Cell. 2007 Aug;13(2):190-202. PMID:17681131 doi:http://dx.doi.org/10.1016/j.devcel.2007.07.002
- ↑ Kim K, Lee S, Chang J, Rhee K. A novel function of CEP135 as a platform protein of C-NAP1 for its centriolar localization. Exp Cell Res. 2008 Dec 10;314(20):3692-700. doi: 10.1016/j.yexcr.2008.09.016., Epub 2008 Oct 1. PMID:18851962 doi:http://dx.doi.org/10.1016/j.yexcr.2008.09.016
- ↑ Kurtulmus B, Wang W, Ruppert T, Neuner A, Cerikan B, Viol L, Duenas-Sanchez R, Gruss OJ, Pereira G. WDR8 is a centriolar satellite and centriole-associated protein that promotes ciliary vesicle docking during ciliogenesis. J Cell Sci. 2016 Feb 1;129(3):621-36. doi: 10.1242/jcs.179713. Epub 2015 Dec 16. PMID:26675238 doi:http://dx.doi.org/10.1242/jcs.179713
- ↑ Kraatz SHW, Bianchi S, Steinmetz MO. Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils. Biosci Rep. 2018 Aug 22. pii: BSR20181073. doi: 10.1042/BSR20181073. PMID:30135143 doi:http://dx.doi.org/10.1042/BSR20181073
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