View source for 7q1e


==CPAP:TUBULIN:IIH5 ALPHAREP COMPLEX==
<StructureSection load='7q1e' size='340' side='right'caption='[[7q1e]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7q1e]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q1E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7q1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q1e OCA], [https://pdbe.org/7q1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q1e RCSB], [https://www.ebi.ac.uk/pdbsum/7q1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q1e ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CENPJ_HUMAN CENPJ_HUMAN] Seckel syndrome;Autosomal recessive primary microcephaly. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/CENPJ_HUMAN CENPJ_HUMAN] Plays an important role in cell division and centrosome function by participating in centriole duplication. Inhibits microtubule nucleation from the centrosome.<ref>PMID:15047868</ref> <ref>PMID:17681131</ref> <ref>PMID:20531387</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microtubule dynamics is regulated by various cellular proteins and perturbed by small-molecule compounds. To what extent the mechanism of the former resembles that of the latter is an open question. We report here structures of tubulin bound to the PN2-3 domain of CPAP, a protein controlling the length of the centrioles. We show that an alpha-helix of the PN2-3 N-terminal region binds and caps the longitudinal surface of the tubulin beta subunit. Moreover, a PN2-3 N-terminal stretch lies in a beta-tubulin site also targeted by fungal and bacterial peptide-like inhibitors of the vinca domain, sharing a very similar binding mode with these compounds. Therefore, our results identify several characteristic features of cellular partners that bind to this site and highlight a structural convergence of CPAP with small-molecule inhibitors of microtubule assembly.

Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.,Campanacci V, Urvoas A, Ammar Khodja L, Aumont-Nicaise M, Noiray M, Lachkar S, Curmi PA, Minard P, Gigant B Proc Natl Acad Sci U S A. 2022 May 10;119(19):e2120098119. doi: , 10.1073/pnas.2120098119. Epub 2022 May 4. PMID:35507869<ref>PMID:35507869</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7q1e" style="background-color:#fffaf0;"></div>

==See Also==
*[[Centromere protein 3D structure|Centromere protein 3D structure]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ovis aries]]
[[Category: Synthetic construct]]
[[Category: Campanacci V]]
[[Category: Gigant b]]