2tma: Difference between revisions

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[[Image:2tma.gif|left|200px]]<br /><applet load="2tma" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2tma, resolution 15.0&Aring;" />
'''TROPOMYOSIN CRYSTAL STRUCTURE AND MUSCLE REGULATION. APPENDIX. CONSTRUCTION OF AN ATOMIC MODEL FOR TROPOMYOSIN AND IMPLICATIONS FOR INTERACTIONS WITH ACTIN'''<br />


==About this Structure==
==TROPOMYOSIN CRYSTAL STRUCTURE AND MUSCLE REGULATION. APPENDIX. CONSTRUCTION OF AN ATOMIC MODEL FOR TROPOMYOSIN AND IMPLICATIONS FOR INTERACTIONS WITH ACTIN==
2TMA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TMA OCA].  
<StructureSection load='2tma' size='340' side='right'caption='[[2tma]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2tma]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TMA 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]] 15&#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=2tma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tma OCA], [https://pdbe.org/2tma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tma RCSB], [https://www.ebi.ac.uk/pdbsum/2tma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tma ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPM1_RABIT TPM1_RABIT] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
== 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/tm/2tma_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=2tma ConSurf].
<div style="clear:both"></div>


==Reference==
==See Also==
Construction of an atomic model for tropomyosin and implications for interactions with actin., Phillips GN Jr, J Mol Biol. 1986 Nov 5;192(1):128-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3820300 3820300]
*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Cohen C]]
[[Category: Cohen, C.]]
[[Category: Phillips Jr GN]]
[[Category: Phillipsjunior, G N.]]
[[Category: contractile system protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:47 2008''

Latest revision as of 09:24, 21 February 2024

TROPOMYOSIN CRYSTAL STRUCTURE AND MUSCLE REGULATION. APPENDIX. CONSTRUCTION OF AN ATOMIC MODEL FOR TROPOMYOSIN AND IMPLICATIONS FOR INTERACTIONS WITH ACTIN

2tma, resolution 15.00Å

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