4rs6: Difference between revisions

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==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==
==Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens==
<StructureSection load='4rs6' size='340' side='right' caption='[[4rs6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4rs6' size='340' side='right'caption='[[4rs6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4rs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4rs6]] 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=4RS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RS6 FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </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]] 2.6&#8491;</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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [http://pdbe.org/4rs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rs6 PDBsum]</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=4rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rs6 OCA], [https://pdbe.org/4rs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rs6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rs6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN]] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>
[https://www.uniprot.org/uniprot/PLK2_HUMAN PLK2_HUMAN] Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.<ref>PMID:15242618</ref> <ref>PMID:19001868</ref> <ref>PMID:20531387</ref> <ref>PMID:20352051</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Polo kinase]]
[[Category: Homo sapiens]]
[[Category: Quan, J]]
[[Category: Large Structures]]
[[Category: Shan, H]]
[[Category: Quan J]]
[[Category: Wang, T]]
[[Category: Shan H]]
[[Category: First pbd domain of polo like kinase ii]]
[[Category: Wang T]]
[[Category: Phosphorylation of target protein]]
[[Category: Transferase]]

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