View source for 6lxp


==TvCyP2 in apo form 2==
<StructureSection load='6lxp' size='340' side='right'caption='[[6lxp]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lxp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LXP 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]] 2.35&#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=6lxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lxp OCA], [https://pdbe.org/6lxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lxp RCSB], [https://www.ebi.ac.uk/pdbsum/6lxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lxp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2DLL4_TRIV3 A2DLL4_TRIV3] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Trichomonas vaginalis (T. vaginalis), cyclophilins play a vital role in dislodging Myb proteins from the membrane compartment and leading them to nuclear translocation. We previously reported that TvCyP1 cyclophilin from T. vaginalis forms a dimer and plays an essential role in moving the Myb1 transcription factor toward the nucleus. In comparison, TvCyP2 containing an extended segment at the N-terminus (N-terminal segment) formed a monomer and showed a different role in regulating protein trafficking. Four X-ray structures of TvCyP2 were determined under various conditions, all showing the N-terminal segment interacting with the active site of a neighboring TvCyP2, an unusual interaction. NMR study revealed that this particular interaction exists in solution as well and also the N-terminal segment seems to interact with the membrane. In vivo study of TvCyP2 and TvCyP2-N (TvCyP2 without the N-terminal segment) indicated that both proteins have different subcellular localization. Together, the structural and functional characteristics at the N-terminal segment offer valuable information for insights into the mechanism of how TvCyP2 regulates protein trafficking, which may be applied in drug development to prevent pathogenesis and disease progression in T. vaginalis infection.

N-Terminal Segment of TvCyP2 Cyclophilin from Trichomonas vaginalis Is Involved in Self-Association, Membrane Interaction, and Subcellular Localization.,Aryal S, Hsu HM, Lou YC, Chu CH, Tai JH, Hsu CH, Chen C Biomolecules. 2020 Aug 26;10(9). pii: biom10091239. doi: 10.3390/biom10091239. PMID:32859063<ref>PMID:32859063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lxp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trichomonas vaginalis]]
[[Category: Aryal S]]
[[Category: Chen C]]
[[Category: Hsu CH]]