6z4z: Difference between revisions
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==Crystal structure of CLK1 in complex with macrocycle ODS2004070== | ==Crystal structure of CLK1 in complex with macrocycle ODS2004070== | ||
<StructureSection load='6z4z' size='340' side='right'caption='[[6z4z]]' scene=''> | <StructureSection load='6z4z' size='340' side='right'caption='[[6z4z]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z4Z FirstGlance]. <br> | <table><tr><td colspan='2'>[[6z4z]] is a 3 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=6Z4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z4Z 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=6z4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z4z OCA], [https://pdbe.org/6z4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z4z RCSB], [https://www.ebi.ac.uk/pdbsum/6z4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z4z 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]] 2.07Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PQ5:7,10-Dioxa-13,17,18,21-tetrazatetracyclo[12.5.2.12,6.017,20]docosa-1(20),2(22),3,5,14(21),15,18-heptaene-5-carboxylic+acid'>PQ5</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=6z4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z4z OCA], [https://pdbe.org/6z4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z4z RCSB], [https://www.ebi.ac.uk/pdbsum/6z4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z4z ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CLK1_HUMAN CLK1_HUMAN] Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.<ref>PMID:10480872</ref> <ref>PMID:19168442</ref> | |||
==See Also== | ==See Also== | ||
*[[Dual specificity protein kinase 3D structures|Dual specificity protein kinase 3D structures]] | *[[Dual specificity protein kinase 3D structures|Dual specificity protein kinase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Benderitter P]] | [[Category: Benderitter P]] |
Latest revision as of 16:41, 24 January 2024
Crystal structure of CLK1 in complex with macrocycle ODS2004070Crystal structure of CLK1 in complex with macrocycle ODS2004070
Structural highlights
FunctionCLK1_HUMAN Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.[1] [2] See AlsoReferences
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