5fcn

From Proteopedia

(Difference between revisions)

Current revision

microtubule binding domain of human CEP135

Structural highlights

5fcn 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 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Centrioles are microtubule-based structures that play important roles notably in cell division and cilium biogenesis. CEP135/Bld10p family members are evolutionarily conserved microtubule-binding proteins important for centriole formation. Here, we analyzed in detail the microtubule-binding activity of human CEP135 (HsCEP135). X-ray crystallography and small-angle X-ray scattering in combination with molecular modeling revealed that the 158 N-terminal residues of HsCEP135 (HsCEP135-N) form a parallel two-stranded coiled-coil structure. Biochemical, cryo-electron, and fluorescence microscopy analyses revealed that in vitro HsCEP135-N interacts with tubulin, protofilaments, and microtubules and induces the formation of microtubule bundles. We further identified a 13 amino acid segment spanning residues 96-108, which represents a major microtubule-binding site in HsCEP135-N. Within this segment, we identified a cluster of three lysine residues that contribute to the microtubule bundling activity of HsCEP135-N. Our results provide the first structural information on CEP135/Bld10p proteins and offer insights into their microtubule-binding mechanism.

The Human Centriolar Protein CEP135 Contains a Two-Stranded Coiled-Coil Domain Critical for Microtubule Binding.,Kraatz S, Guichard P, Obbineni JM, Olieric N, Hatzopoulos GN, Hilbert M, Sen I, Missimer J, Gonczy P, Steinmetz MO Structure. 2016 Jul 20. pii: S0969-2126(16)30138-1. doi:, 10.1016/j.str.2016.06.011. PMID:27477386^[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 S, Guichard P, Obbineni JM, Olieric N, Hatzopoulos GN, Hilbert M, Sen I, Missimer J, Gonczy P, Steinmetz MO. The Human Centriolar Protein CEP135 Contains a Two-Stranded Coiled-Coil Domain Critical for Microtubule Binding. Structure. 2016 Jul 20. pii: S0969-2126(16)30138-1. doi:, 10.1016/j.str.2016.06.011. PMID:27477386 doi:http://dx.doi.org/10.1016/j.str.2016.06.011

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/5fcn"

Categories: Homo sapiens | Large Structures | Kraatz SHW

@@ Line 3: / Line 3: @@
 <StructureSection load='5fcn' size='340' side='right'caption='[[5fcn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5fcn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FCN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FCN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5fcn]] 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=5FCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FCN FirstGlance]. <br>
-</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=5fcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fcn OCA], [http://pdbe.org/5fcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fcn RCSB], [http://www.ebi.ac.uk/pdbsum/5fcn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fcn 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]] 1.8&#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=5fcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fcn OCA], [https://pdbe.org/5fcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fcn RCSB], [https://www.ebi.ac.uk/pdbsum/5fcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fcn ProSAT]</span></td></tr>
 </table>
 == 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 ==
-[[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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Kraatz, S H.W]]
+[[Category: Kraatz SHW]]
-[[Category: Centriole]]
-[[Category: Coiled-coil]]
-[[Category: Microtubule-binding protein]]

5fcn

From Proteopedia

Current revision

microtubule binding domain of human CEP135

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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