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< | ==COMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES OF THE EF HAND PARVALBUMIN== | ||
<StructureSection load='2pas' size='340' side='right'caption='[[2pas]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2pas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Esox_lucius Esox lucius]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PAS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 9 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=2pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pas OCA], [https://pdbe.org/2pas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pas RCSB], [https://www.ebi.ac.uk/pdbsum/2pas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pas ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRVA_ESOLU PRVA_ESOLU] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. | |||
== 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/pa/2pas_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2pas ConSurf]. | |||
<div style="clear:both"></div> | |||
== | ==See Also== | ||
*[[Parvalbumin|Parvalbumin]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Esox lucius]] | [[Category: Esox lucius]] | ||
[[Category: Baldellon | [[Category: Large Structures]] | ||
[[Category: Cave | [[Category: Baldellon C]] | ||
[[Category: Etienne | [[Category: Cave A]] | ||
[[Category: Padilla | [[Category: Etienne G]] | ||
[[Category: Parello | [[Category: Padilla A]] | ||
[[Category: Parello J]] | |||
Latest revision as of 08:25, 17 October 2024
COMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES OF THE EF HAND PARVALBUMINCOMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES OF THE EF HAND PARVALBUMIN
Structural highlights
FunctionPRVA_ESOLU In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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