1ul7

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(New page: 200px<br /><applet load="1ul7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ul7" /> '''Solution structure of kinase associated doma...)
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[[Image:1ul7.jpg|left|200px]]<br /><applet load="1ul7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ul7" />
 
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'''Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3'''<br />
 
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==Overview==
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==Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3==
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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.
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<StructureSection load='1ul7' size='340' side='right'caption='[[1ul7]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ul7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ul7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:17075132</ref>
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1UL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UL7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17075132 17075132]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1ul7" style="background-color:#fffaf0;"></div>
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Single protein]]
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[[Category: Kigawa, T.]]
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[[Category: Koshiba, S.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: Tochio, N.]]
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[[Category: Yokoyama, S.]]
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[[Category: elkl motif]]
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[[Category: ka1 domain]]
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[[Category: mark3]]
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[[Category: national project on protein structural and functional analyses]]
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[[Category: nppsfa]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:13:03 2007''
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==See Also==
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Kigawa T]]
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[[Category: Koshiba S]]
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[[Category: Tochio N]]
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[[Category: Yokoyama S]]

Current revision

Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3

PDB ID 1ul7

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