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5efq
From Proteopedia
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| - | ''' | + | ==Crystal structure of human Cdk13/Cyclin K in complex with ADP-aluminum fluoride== |
| - | + | <StructureSection load='5efq' size='340' side='right' caption='[[5efq]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5efq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EFQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=5efq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efq OCA], [http://pdbe.org/5efq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5efq RCSB], [http://www.ebi.ac.uk/pdbsum/5efq PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CDK13_HUMAN CDK13_HUMAN]] Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef.<ref>PMID:16721827</ref> <ref>PMID:1731328</ref> <ref>PMID:18480452</ref> <ref>PMID:20952539</ref> [[http://www.uniprot.org/uniprot/CCNK_HUMAN CCNK_HUMAN]] May play a role in transcriptional regulation. In vitro, is associated with a kinase activity toward both RNA polymerase II C-terminal domain and CDK2 (CAK).<ref>PMID:10574912</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Anand, K]] | [[Category: Anand, K]] | ||
| - | [[Category: Greifenberg, A.K]] | ||
[[Category: Geyer, M]] | [[Category: Geyer, M]] | ||
| + | [[Category: Greifenberg, A K]] | ||
[[Category: Hoenig, D]] | [[Category: Hoenig, D]] | ||
| + | [[Category: Adp]] | ||
| + | [[Category: Cyclin]] | ||
| + | [[Category: Kinase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 19:39, 30 December 2015
Crystal structure of human Cdk13/Cyclin K in complex with ADP-aluminum fluoride
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Categories: Anand, K | Geyer, M | Greifenberg, A K | Hoenig, D | Adp | Cyclin | Kinase | Transferase
