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4rs6

From Proteopedia

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Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens

Structural highlights

4rs6 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 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Polo-like kinase 2 (PLK2) is a crucial regulator in cell cycle progression, DNA damage response, and neuronal activity. PLK2 is characterized by the conserved N-terminal kinase domain and the unique C-terminal polo-box domain (PBD). The PBD mediates diverse functions of PLK2 by binding phosphorylated Ser-pSer/pThr motifs of its substrates. Here, we report the first crystal structure of the PBD of PLK2. The overall structure of the PLK2 PBD is similar to that of the PLK1 PBD, which is composed by two polo boxes each contain beta6alpha structures that form a 12-stranded beta sandwich domain. The edge of the interface between the two polo boxes forms the phosphorylated Ser-pSer/pThr motifs binding cleft. On the hand, the peripheral regions around the core binding cleft of the PLK2 PBD is distinct from that of the PLK1 PBD, which might confer the substrate specificity of the PBDs of the polo-like kinase family.

Crystal structure of the polo-box domain of polo-like kinase 2.,Shan HM, Wang T, Quan JM Biochem Biophys Res Commun. 2015 Jan 16;456(3):780-4. doi:, 10.1016/j.bbrc.2014.11.125. Epub 2014 Dec 13. PMID:25511705^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Warnke S, Kemmler S, Hames RS, Tsai HL, Hoffmann-Rohrer U, Fry AM, Hoffmann I. Polo-like kinase-2 is required for centriole duplication in mammalian cells. Curr Biol. 2004 Jul 13;14(13):1200-7. PMID:15242618 doi:10.1016/j.cub.2004.06.059
↑ Cizmecioglu O, Warnke S, Arnold M, Duensing S, Hoffmann I. Plk2 regulated centriole duplication is dependent on its localization to the centrioles and a functional polo-box domain. Cell Cycle. 2008 Nov 15;7(22):3548-55. Epub 2008 Nov 26. PMID:19001868
↑ Chang J, Cizmecioglu O, Hoffmann I, Rhee K. PLK2 phosphorylation is critical for CPAP function in procentriole formation during the centrosome cycle. EMBO J. 2010 Jul 21;29(14):2395-406. doi: 10.1038/emboj.2010.118. Epub 2010 Jun, 8. PMID:20531387 doi:10.1038/emboj.2010.118
↑ Krause A, Hoffmann I. Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication. PLoS One. 2010 Mar 24;5(3):e9849. doi: 10.1371/journal.pone.0009849. PMID:20352051 doi:10.1371/journal.pone.0009849
↑ Shan HM, Wang T, Quan JM. Crystal structure of the polo-box domain of polo-like kinase 2. Biochem Biophys Res Commun. 2015 Jan 16;456(3):780-4. doi:, 10.1016/j.bbrc.2014.11.125. Epub 2014 Dec 13. PMID:25511705 doi:http://dx.doi.org/10.1016/j.bbrc.2014.11.125

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rs6"

Categories: Homo sapiens | Large Structures | Quan J | Shan H | Wang T

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <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='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>
+</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'>[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>
 == Function ==

4rs6

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Current revision

Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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