5lhx

From Proteopedia

(Difference between revisions)

Revision as of 07:22, 9 March 2017

PB3 Domain of Drosophila melanogaster PLK4 (Sak)

Structural highlights

5lhx is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Polo kinase, with EC number 2.7.11.21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PLK4_DROME] Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.^[1] ^[2] ^[3]

Publication Abstract from PubMed

A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of Plk4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of Plk4 and the coiled-coil domain of STIL (HsCCD). We showed previously that the Drosophila Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer in vitro that likely precludes an interaction with PB3. Here we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers in vitro, but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although Drosophila PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD in vitro Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.

A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies.,Cottee MA, Johnson S, Raff JW, Lea SM Biol Open. 2017 Feb 15. pii: bio.024661. doi: 10.1242/bio.024661. PMID:28202467^[4]

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

References

↑ Bettencourt-Dias M, Rodrigues-Martins A, Carpenter L, Riparbelli M, Lehmann L, Gatt MK, Carmo N, Balloux F, Callaini G, Glover DM. SAK/PLK4 is required for centriole duplication and flagella development. Curr Biol. 2005 Dec 20;15(24):2199-207. Epub 2005 Dec 1. PMID:16326102 doi:http://dx.doi.org/10.1016/j.cub.2005.11.042
↑ Rodrigues-Martins A, Riparbelli M, Callaini G, Glover DM, Bettencourt-Dias M. Revisiting the role of the mother centriole in centriole biogenesis. Science. 2007 May 18;316(5827):1046-50. Epub 2007 Apr 26. PMID:17463247 doi:http://dx.doi.org/10.1126/science.1142950
↑ Basto R, Brunk K, Vinadogrova T, Peel N, Franz A, Khodjakov A, Raff JW. Centrosome amplification can initiate tumorigenesis in flies. Cell. 2008 Jun 13;133(6):1032-42. doi: 10.1016/j.cell.2008.05.039. PMID:18555779 doi:http://dx.doi.org/10.1016/j.cell.2008.05.039
↑ Cottee MA, Johnson S, Raff JW, Lea SM. A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies. Biol Open. 2017 Feb 15. pii: bio.024661. doi: 10.1242/bio.024661. PMID:28202467 doi:http://dx.doi.org/10.1242/bio.024661

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lhx"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5lhx is ON HOLD  until Paper Publication
+==PB3 Domain of Drosophila melanogaster PLK4 (Sak)==
+<StructureSection load='5lhx' size='340' side='right' caption='[[5lhx]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5lhx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHX 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>
+<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=5lhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhx OCA], [http://pdbe.org/5lhx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhx RCSB], [http://www.ebi.ac.uk/pdbsum/5lhx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PLK4_DROME PLK4_DROME]] Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.<ref>PMID:16326102</ref> <ref>PMID:17463247</ref> <ref>PMID:18555779</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of Plk4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of Plk4 and the coiled-coil domain of STIL (HsCCD). We showed previously that the Drosophila Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer in vitro that likely precludes an interaction with PB3. Here we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers in vitro, but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although Drosophila PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD in vitro Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.
-Authors:
+A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies.,Cottee MA, Johnson S, Raff JW, Lea SM Biol Open. 2017 Feb 15. pii: bio.024661. doi: 10.1242/bio.024661. PMID:28202467<ref>PMID:28202467</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5lhx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Polo kinase]]
+[[Category: Cottee, M A]]
+[[Category: Lea, S M]]
+[[Category: Centriole]]
+[[Category: Polo box domain]]
+[[Category: Structural protein]]
+[[Category: Transferase]]

5lhx

From Proteopedia

Revision as of 07:22, 9 March 2017

PB3 Domain of Drosophila melanogaster PLK4 (Sak)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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