31hp: Difference between revisions
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==Crystal structure of tau tubulin kinase 2 (TTBK2) in complex with compound 62== | |||
<StructureSection load='31hp' size='340' side='right'caption='[[31hp]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[31hp]] is a 1 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=31HP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=31HP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1J95:~{N}-[4-(furan-2-yl)phenyl]-7~{H}-pyrrolo[2,3-d]pyrimidin-4-amine'>A1J95</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=31hp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=31hp OCA], [https://pdbe.org/31hp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=31hp RCSB], [https://www.ebi.ac.uk/pdbsum/31hp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=31hp ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Disease == | ||
[[Category: Martinez | [https://www.uniprot.org/uniprot/TTBK2_HUMAN TTBK2_HUMAN] Spinocerebellar ataxia type 11. The disease is caused by mutations affecting the gene represented in this entry. | ||
[[Category: Sanchez-Santos | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/TTBK2_HUMAN TTBK2_HUMAN] Serine/threonine kinase that acts as a key regulator of ciliogenesis: controls the initiation of ciliogenesis by binding to the distal end of the basal body and promoting the removal of CCP110, which caps the mother centriole, leading to the recruitment of IFT proteins, which build the ciliary axoneme. Has some substrate preference for proteins that are already phosphorylated on a Tyr residue at the +2 position relative to the phosphorylation site. Able to phosphorylate tau on serines in vitro.<ref>PMID:21548880</ref> <ref>PMID:23141541</ref> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Joerger AC]] | |||
[[Category: Knapp S]] | |||
[[Category: Martinez A]] | |||
[[Category: Sanchez-Santos C]] | |||
[[Category: Zhubi R]] | |||
Latest revision as of 19:57, 29 July 2026
Crystal structure of tau tubulin kinase 2 (TTBK2) in complex with compound 62
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