4yyp: Difference between revisions

New page: '''Unreleased structure''' The entry 4yyp is ON HOLD until Paper Publication Authors: Imseng, S., Arquint, C., Gabryjonczyk, A., Boehm, R., Sauer, E., Hiller, S., Nigg, E.A., Maier, T. ...
 
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'''Unreleased structure'''


The entry 4yyp is ON HOLD  until Paper Publication
==Crystal structure of human PLK4-PB3 in complex with STIL-CC==
<StructureSection load='4yyp' size='340' side='right'caption='[[4yyp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yyp]] 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=4YYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YYP 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4yyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yyp OCA], [https://pdbe.org/4yyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yyp RCSB], [https://www.ebi.ac.uk/pdbsum/4yyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yyp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PLK4_HUMAN PLK4_HUMAN] Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2.<ref>PMID:16326102</ref> <ref>PMID:16244668</ref> <ref>PMID:17681131</ref> <ref>PMID:18239451</ref> <ref>PMID:19164942</ref> <ref>PMID:21725316</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Polo-like kinases (PLK) are eukaryotic regulators of cell cycle progression, mitosis and cytokinesis; PLK4 is a master regulator of centriole duplication. Here, we demonstrate that the SCL/TAL1 interrupting locus (STIL) protein interacts via its coiled-coil region (STIL-CC) with PLK4 in vivo. STIL-CC is the first identified interaction partner of Polo-box 3 (PB3) of PLK4 and also uses a secondary interaction site in the PLK4 L1 region. Structure determination of free PLK4-PB3 and its STIL-CC complex via NMR and crystallography reveals a novel mode of Polo-box-peptide interaction mimicking coiled-coil formation. In vivo analysis of structure-guided STIL mutants reveals distinct binding modes to PLK4-PB3 and L1, as well as interplay of STIL oligomerization with PLK4 binding. We suggest that the STIL-CC/PLK4 interaction mediates PLK4 activation as well as stabilization of centriolar PLK4 and plays a key role in centriole duplication.


Authors: Imseng, S., Arquint, C., Gabryjonczyk, A., Boehm, R., Sauer, E., Hiller, S., Nigg, E.A., Maier, T.
STIL binding to Polo-box 3 of PLK4 regulates centriole duplication.,Arquint C, Gabryjonczyk AM, Imseng S, Bohm R, Sauer E, Hiller S, Nigg EA, Maier T Elife. 2015 Jul 18;4. doi: 10.7554/eLife.07888. PMID:26188084<ref>PMID:26188084</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Boehm, R]]
<div class="pdbe-citations 4yyp" style="background-color:#fffaf0;"></div>
[[Category: Hiller, S]]
 
[[Category: Imseng, S]]
==See Also==
[[Category: Gabryjonczyk, A]]
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
[[Category: Sauer, E]]
== References ==
[[Category: Maier, T]]
<references/>
[[Category: Nigg, E.A]]
__TOC__
[[Category: Arquint, C]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arquint C]]
[[Category: Boehm R]]
[[Category: Gabryjonczyk A]]
[[Category: Hiller S]]
[[Category: Imseng S]]
[[Category: Maier T]]
[[Category: Nigg EA]]
[[Category: Sauer E]]

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