2cqb: Difference between revisions
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==Solution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase E== | |||
<StructureSection load='2cqb' size='340' side='right'caption='[[2cqb]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2cqb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CQB 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=2cqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cqb OCA], [https://pdbe.org/2cqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cqb RCSB], [https://www.ebi.ac.uk/pdbsum/2cqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cqb ProSAT], [https://www.topsan.org/Proteins/RSGI/2cqb TOPSAN]</span></td></tr> | ||
[[2cqb]] is a 1 chain structure | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PPIE_HUMAN PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. | |||
== 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/cq/2cqb_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=2cqb ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Cyclophilin|Cyclophilin]] | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Inoue | [[Category: Inoue M]] | ||
[[Category: Kigawa | [[Category: Kigawa T]] | ||
[[Category: Muto | [[Category: Muto Y]] | ||
[[Category: Shirouzu M]] | |||
[[Category: Shirouzu | [[Category: Someya T]] | ||
[[Category: Someya | [[Category: Terada T]] | ||
[[Category: Terada | [[Category: Yokoyama S]] | ||
[[Category: Yokoyama | |||
Latest revision as of 14:28, 22 May 2024
Solution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase ESolution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase E
Structural highlights
FunctionPPIE_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. 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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