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[[Image:3lpy.png|left|200px]]


{{STRUCTURE_3lpy|  PDB=3lpy  |  SCENE=  }}
==Crystal structure of the RRM domain of CyP33==
 
<StructureSection load='3lpy' size='340' side='right'caption='[[3lpy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
===Crystal structure of the RRM domain of CyP33===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3lpy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LPY FirstGlance]. <br>
{{ABSTRACT_PUBMED_20541251}}
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lpy OCA], [https://pdbe.org/3lpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lpy RCSB], [https://www.ebi.ac.uk/pdbsum/3lpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lpy ProSAT]</span></td></tr>
[[3lpy]] is a 2 chain structure of [[Cyclophilin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPY OCA].  
</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/lp/3lpy_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=3lpy ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Cyclophilin|Cyclophilin]]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:020541251</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Patel, D J.]]
[[Category: Patel DJ]]
[[Category: Wang, Z.]]
[[Category: Wang Z]]
[[Category: Cyp33]]
[[Category: Isomerase]]
[[Category: Mll1 binding]]
[[Category: Mrna processing]]
[[Category: Mrna splicing]]
[[Category: Nucleus]]
[[Category: Rna-binding]]
[[Category: Rotamase]]
[[Category: Rrm]]
[[Category: Spliceosome]]

Latest revision as of 13:21, 21 February 2024

Crystal structure of the RRM domain of CyP33Crystal structure of the RRM domain of CyP33

Structural highlights

3lpy is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3lpy, resolution 2.00Å

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