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| | ==Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3== | | ==Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3== |
| - | <StructureSection load='1ul7' size='340' side='right'caption='[[1ul7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1ul7' size='340' side='right'caption='[[1ul7]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ul7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ul7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UL7 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIKEN cDNA 1600015G02, Mark3, Emk2, Mpk10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=1ul7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul7 OCA], [https://pdbe.org/1ul7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ul7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ul7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ul7 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ul7 TOPSAN]</span></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=1ul7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul7 OCA], [https://pdbe.org/1ul7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ul7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ul7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ul7 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ul7 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MARK3_MOUSE MARK3_MOUSE]] Involved in the specific phosphorylation of microtubule-associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (By similarity).
| + | [https://www.uniprot.org/uniprot/MARK3_MOUSE MARK3_MOUSE] Involved in the specific phosphorylation of microtubule-associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Kigawa T]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Koshiba S]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Tochio N]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Yokoyama S]] |
| - | [[Category: Tochio, N]] | + | |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Elkl motif]]
| + | |
| - | [[Category: Ka1 domain]]
| + | |
| - | [[Category: Mark3]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
MARK3_MOUSE Involved in the specific phosphorylation of microtubule-associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Microtubule-associated protein/microtubule affinity-regulating kinases (MARKs)/PAR-1 are common regulators of cell polarity that are conserved from nematode to human. All of these kinases have a highly conserved C-terminal domain, which is termed the kinase-associated domain 1 (KA1), although its function is unknown. In this study, we determined the solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy. We found that approximately 50 additional residues preceding the previously defined KA1 domain are required for its proper folding. The newly defined KA1 domain adopts a compact alpha+beta structure with a betaalphabetabetabetabetaalpha topology. We also found a characteristic hydrophobic, concave surface surrounded by positively charged residues. This concave surface includes the highly conserved Glu-Leu-Lys-Leu motif at the C terminus, indicating that it is important for the function of the KA1 domain.
Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3.,Tochio N, Koshiba S, Kobayashi N, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Motoda Y, Kobayashi A, Tanaka A, Hayashizaki Y, Terada T, Shirouzu M, Kigawa T, Yokoyama S Protein Sci. 2006 Nov;15(11):2534-43. PMID:17075132[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tochio N, Koshiba S, Kobayashi N, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Motoda Y, Kobayashi A, Tanaka A, Hayashizaki Y, Terada T, Shirouzu M, Kigawa T, Yokoyama S. Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3. Protein Sci. 2006 Nov;15(11):2534-43. PMID:17075132 doi:15/11/2534
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