2dml: Difference between revisions
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== | ==The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A6== | ||
<StructureSection load='2dml' size='340' side='right'caption='[[2dml]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2dml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DML FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2dml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dml OCA], [https://pdbe.org/2dml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dml RCSB], [https://www.ebi.ac.uk/pdbsum/2dml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dml ProSAT], [https://www.topsan.org/Proteins/RSGI/2dml TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PDIA6_MOUSE PDIA6_MOUSE] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity). | |||
== 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/dm/2dml_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=2dml ConSurf]. | |||
<div style="clear:both"></div> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Inoue M]] | |||
[[Category: Kigawa T]] | |||
[[Category: Inoue | [[Category: Koshiba S]] | ||
[[Category: Kigawa | [[Category: Tochio N]] | ||
[[Category: Koshiba | [[Category: Yokoyama S]] | ||
[[Category: Tochio | |||
[[Category: Yokoyama | |||
Latest revision as of 21:44, 29 May 2024
The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A6The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A6
Structural highlights
FunctionPDIA6_MOUSE May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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