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7z0g
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==CPAP:TUBULIN:IE5 ALPHAREP COMPLEX P1 SPACE GROUP== |
| - | <StructureSection load='7z0g' size='340' side='right'caption='[[7z0g]]' scene=''> | + | <StructureSection load='7z0g' size='340' side='right'caption='[[7z0g]], [[Resolution|resolution]] 3.49Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7z0g]] is a 8 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=7Z0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z0G FirstGlance]. <br> |
| - | </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=7z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z0g OCA], [https://pdbe.org/7z0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z0g RCSB], [https://www.ebi.ac.uk/pdbsum/7z0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z0g 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]] 3.487Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=7z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z0g OCA], [https://pdbe.org/7z0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z0g RCSB], [https://www.ebi.ac.uk/pdbsum/7z0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z0g ProSAT]</span></td></tr> | ||
</table> | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7z0g" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Centromere protein 3D structure|Centromere protein 3D structure]] | ||
| + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Ovis aries]] |
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Campanacci V]] | ||
| + | [[Category: Gigant B]] | ||
Current revision
CPAP:TUBULIN:IE5 ALPHAREP COMPLEX P1 SPACE GROUP
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