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4j7b
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(Difference between revisions)
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| - | + | ==Crystal structure of polo-like kinase 1== | |
| - | === | + | <StructureSection load='4j7b' size='340' side='right' caption='[[4j7b]], [[Resolution|resolution]] 2.30Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4j7b]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J7B FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plk1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Danio rerio]), Map205, CG1483 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</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=4j7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j7b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j7b RCSB], [http://www.ebi.ac.uk/pdbsum/4j7b PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polo-like kinase 1 (PLK1) is a master regulator of mitosis and is considered a potential drug target for cancer therapy. PLK1 is characterized by an N-terminal kinase domain (KD) and a C-terminal Polo-box domain (PBD). The KD and PBD are mutually inhibited, but the molecular mechanisms of the autoinhibition remain unclear. Here we report the 2.3-A crystal structure of the complex of the Danio rerio KD and PBD together with a PBD-binding motif of Drosophila melanogaster microtubule-associated protein 205 (Map205(PBM)). The structure reveals that the PBD binds and rigidifies the hinge region of the KD in a distinct conformation from that of the phosphopeptide-bound PBD. This structure provides a framework for understanding the autoinhibitory mechanisms of PLK1 and also sheds light on the activation mechanisms of PLK1 by phosphorylation or phosphopeptide binding. | ||
| - | + | Structural basis for the inhibition of Polo-like kinase 1.,Xu J, Shen C, Wang T, Quan J Nat Struct Mol Biol. 2013 Sep;20(9):1047-53. doi: 10.1038/nsmb.2623. Epub 2013, Jul 28. PMID:23893132<ref>PMID:23893132</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Danio rerio]] | [[Category: Danio rerio]] | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Polo kinase]] | [[Category: Polo kinase]] | ||
| - | [[Category: Quan, J | + | [[Category: Quan, J]] |
| - | [[Category: Shen, C | + | [[Category: Shen, C]] |
| - | [[Category: Wang, T | + | [[Category: Wang, T]] |
| - | [[Category: Xu, J | + | [[Category: Xu, J]] |
[[Category: First complex structure of kd and pbd domain]] | [[Category: First complex structure of kd and pbd domain]] | ||
[[Category: Phosphorylated target protein]] | [[Category: Phosphorylated target protein]] | ||
[[Category: Regulator of mitosis]] | [[Category: Regulator of mitosis]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 12:06, 21 December 2014
Crystal structure of polo-like kinase 1
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