1tlk: Difference between revisions

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{{Seed}}
[[Image:1tlk.png|left|200px]]


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==X-RAY STRUCTURE DETERMINATION OF TELOKIN, THE C-TERMINAL DOMAIN OF MYOSIN LIGHT CHAIN KINASE, AT 2.8 ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_1tlk", creates the "Structure Box" on the page.
<StructureSection load='1tlk' size='340' side='right'caption='[[1tlk]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1tlk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLK FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#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=1tlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tlk OCA], [https://pdbe.org/1tlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tlk RCSB], [https://www.ebi.ac.uk/pdbsum/1tlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tlk ProSAT]</span></td></tr>
{{STRUCTURE_1tlk|  PDB=1tlk  |  SCENE=  }}
</table>
 
== Function ==
===X-RAY STRUCTURE DETERMINATION OF TELOKIN, THE C-TERMINAL DOMAIN OF MYOSIN LIGHT CHAIN KINASE, AT 2.8 ANGSTROMS RESOLUTION===
[https://www.uniprot.org/uniprot/MYLK_MELGA MYLK_MELGA] Corresponds to the C-terminus of smooth muscle myosin light chain kinase.
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
The line below this paragraph, {{ABSTRACT_PUBMED_1404391}}, adds the Publication Abstract to the page
  <jmolCheckbox>
(as it appears on PubMed at http://www.pubmed.gov), where 1404391 is the PubMed ID number.
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tl/1tlk_consurf.spt"</scriptWhenChecked>
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    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
{{ABSTRACT_PUBMED_1404391}}
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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=1tlk ConSurf].
1TLK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLK OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution., Holden HM, Ito M, Hartshorne DJ, Rayment I, J Mol Biol. 1992 Oct 5;227(3):840-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1404391 1404391]
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
[[Category: Single protein]]
[[Category: Holden HM]]
[[Category: Holden, H M.]]
[[Category: Rayment I]]
[[Category: Rayment, I.]]
[[Category: Calmodulin-binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:24:31 2008''

Latest revision as of 08:40, 14 February 2024

X-RAY STRUCTURE DETERMINATION OF TELOKIN, THE C-TERMINAL DOMAIN OF MYOSIN LIGHT CHAIN KINASE, AT 2.8 ANGSTROMS RESOLUTION

1tlk, resolution 2.80Å

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