1kob
From Proteopedia
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| - | [[Image:1kob.gif|left|200px]] | ||
| - | < | + | ==TWITCHIN KINASE FRAGMENT (APLYSIA), AUTOREGULATED PROTEIN KINASE DOMAIN== |
| - | + | <StructureSection load='1kob' size='340' side='right'caption='[[1kob]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1kob]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOB 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]] 2.3Å</td></tr> | |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VAL:VALINE'>VAL</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=1kob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kob OCA], [https://pdbe.org/1kob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kob RCSB], [https://www.ebi.ac.uk/pdbsum/1kob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kob ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q16980_APLCA Q16980_APLCA] | |
| - | + | == Evolutionary Conservation == | |
| - | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ko/1kob_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1kob ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The myosin-associated giant protein kinases twitchin and titin are composed predominantly of fibronectin- and immunoglobulin-like modules. We report the crystal structures of two autoinhibited twitchin kinase fragments, one from Aplysia and a larger fragment from Caenorhabditis elegans containing an additional C-terminal immunoglobulin-like domain. The structure of the longer fragment shows that the immunoglobulin domain contacts the protein kinase domain on the opposite side from the catalytic cleft, laterally exposing potential myosin binding residues. Together, the structures reveal the cooperative interactions between the autoregulatory region and the residues from the catalytic domain involved in protein substrate binding, ATP binding, catalysis and the activation loop, and explain the differences between the observed autoinhibitory mechanism and the one found in the structure of calmodulin-dependent kinase I. | The myosin-associated giant protein kinases twitchin and titin are composed predominantly of fibronectin- and immunoglobulin-like modules. We report the crystal structures of two autoinhibited twitchin kinase fragments, one from Aplysia and a larger fragment from Caenorhabditis elegans containing an additional C-terminal immunoglobulin-like domain. The structure of the longer fragment shows that the immunoglobulin domain contacts the protein kinase domain on the opposite side from the catalytic cleft, laterally exposing potential myosin binding residues. Together, the structures reveal the cooperative interactions between the autoregulatory region and the residues from the catalytic domain involved in protein substrate binding, ATP binding, catalysis and the activation loop, and explain the differences between the observed autoinhibitory mechanism and the one found in the structure of calmodulin-dependent kinase I. | ||
| - | + | Giant protein kinases: domain interactions and structural basis of autoregulation.,Kobe B, Heierhorst J, Feil SC, Parker MW, Benian GM, Weiss KR, Kemp BE EMBO J. 1996 Dec 16;15(24):6810-21. PMID:9003756<ref>PMID:9003756</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1kob" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Aplysia californica]] | [[Category: Aplysia californica]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Benian | + | [[Category: Benian GM]] |
| - | [[Category: Feil | + | [[Category: Feil SC]] |
| - | [[Category: Heierhorst | + | [[Category: Heierhorst J]] |
| - | [[Category: Kemp | + | [[Category: Kemp BE]] |
| - | [[Category: Kobe | + | [[Category: Kobe B]] |
| - | [[Category: Parker | + | [[Category: Parker MW]] |
| - | [[Category: Weiss | + | [[Category: Weiss KR]] |
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Current revision
TWITCHIN KINASE FRAGMENT (APLYSIA), AUTOREGULATED PROTEIN KINASE DOMAIN
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Categories: Aplysia californica | Large Structures | Benian GM | Feil SC | Heierhorst J | Kemp BE | Kobe B | Parker MW | Weiss KR
