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<StructureSection load='1koa' size='340' side='right'caption='[[1koa]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='1koa' size='340' side='right'caption='[[1koa]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1koa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1koa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOA FirstGlance]. <br>
</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=1koa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koa OCA], [https://pdbe.org/1koa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koa RCSB], [https://www.ebi.ac.uk/pdbsum/1koa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koa ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</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=1koa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koa OCA], [https://pdbe.org/1koa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koa RCSB], [https://www.ebi.ac.uk/pdbsum/1koa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/UNC22_CAEEL UNC22_CAEEL]] Regulator of muscle contraction and relaxation. Senses mechanical strain that occurs during muscle activity by unfolding in clearly resolvable steps at differing forces.<ref>PMID:7190524</ref> <ref>PMID:18390597</ref>
[https://www.uniprot.org/uniprot/UNC22_CAEEL UNC22_CAEEL] Regulator of muscle contraction and relaxation. Senses mechanical strain that occurs during muscle activity by unfolding in clearly resolvable steps at differing forces.<ref>PMID:7190524</ref> <ref>PMID:18390597</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1koa ConSurf].
</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=1koa ConSurf].
<div style="clear:both"></div>
<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.
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1koa" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caeel]]
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Benian, G M]]
[[Category: Benian GM]]
[[Category: Feil, S C]]
[[Category: Feil SC]]
[[Category: Heierhorst, J]]
[[Category: Heierhorst J]]
[[Category: Kemp, B E]]
[[Category: Kemp BE]]
[[Category: Kobe, B]]
[[Category: Kobe B]]
[[Category: Parker, M W]]
[[Category: Parker MW]]
[[Category: Weiss, K R]]
[[Category: Weiss KR]]
[[Category: Intrasteric regulation]]
[[Category: Kinase]]
[[Category: Twitchin]]
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