Peptidyl-prolyl cis-trans isomerase

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<StructureSection load='' size='450' side='right' caption='Human PPIase (green) complex with phosphoserine containing peptide (magenta) (PDB code [[1f8a]]).' scene='67/677404/Cv/1'>
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<StructureSection load='' size='350' side='right' caption='Human PPIase (green) complex with phosphoserine containing peptide (magenta) (PDB code [[1f8a]]).' scene='67/677404/Cv/1'>
__TOC__
__TOC__
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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The phosphoserine containing peptide found in the heptad repeat of RNA polymerase II large subunit interacts with the WW domain of PPIase Pin1<ref>PMID:10922246</ref>. <scene name='67/677404/Cv/3'>The phosphoserine containing peptide binding site</scene>. Water molecules shown as red spheres.
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The phosphoserine containing peptide found in the heptad repeat of RNA polymerase II large subunit interacts with the WW domain of PPIase Pin1<ref>PMID:10922246</ref>. <scene name='67/677404/Cv/4'>The phosphoserine containing peptide binding site</scene>. Water molecules are shown as red spheres.
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</StructureSection>
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== 3D Structures of peptidyl-prolyl cis-trans isomerase ==
== 3D Structures of peptidyl-prolyl cis-trans isomerase ==
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[[Peptidyl-prolyl cis-trans isomerase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*PPIase
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**[[3k2c]] – PPIase – ''Encephalitozoon cuniculi''<BR />
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**[[1yw5]] – PPIase – ''Candida albicans''<BR />
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**[[2jv4]] – PPIase A WW domain – ''Emericella nidulans'' - NMR<BR />
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**[[2mc9]] – PPIase – rosy periwinkle - NMR<BR />
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**[[2wlw]] – PPIase CypA domain – ''Macaca mulatta'' <BR />
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**[[5xb0]] – PPIase – ''Pseudomonas syringae''<BR />
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**[[4s1e]], [[4s1j]] – PPIase (mutant) – ''Leishmania donovani''<BR />
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**[[2m08]] – PPIase – ''Nitrosopumilus maritimus'' - NMR<BR />
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*PPIase Pin1
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**[[1pin]] – hPin1 – human<BR />
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**[[1nmv]] – hPin1 - NMR<BR />
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**[[1zcn]], [[2zqs]], [[2zqt]], [[2zqu]], [[2zqv]], [[2zr4]], [[2zr5]], [[2zr6]] – hPin1 (mutant)<BR />
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**[[1i6c]], [[2kcf]], [[2kbu]], [[1eq3]], [[2m8i]], [[2m8j]] – hPin1 WW domain - NMR<BR />
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**[[2f21]], [[1fjd]], [[2m9e]], [[2m9f]], [[2m9i]], [[2m9j]] – hPin1 WW domain (mutant)<BR />
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**[[3ik8]] – hPin1 PPIase domain (mutant)<BR />
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**[[2rud]] – hPin1 PPIase domain (mutant) - NMR<BR />
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**[[1nmw]], [[2ruc]] – hPin1 PPIase domain - NMR<BR />
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**[[1j6y]] – Pin1 – ''Arabidopsis thaliana'' - NMR<BR />
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*PPIase Pin1 complexes
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**[[1f8a]] – hPin1 + phosphoserine containing peptide<BR />
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**[[1i8g]], [[1i8h]] – hPin1 WW domain + phosphothreoniine containing peptide - NMR<BR />
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**[[2lb3]] – hPin1 WW domain + MAD homolog peptide - NMR<BR />
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**[[4gwt]], [[4gwv]] – hPin1 WW domain + small molecule<BR />
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**[[2itk]] – hPin1 (mutant) + D-peptide<BR />
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**[[2q5a]] – hPin1 (mutant) + L-peptide<BR />
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**[[3ikd]], [[3ikg]], [[3kac]], [[3jyj]], [[3i6c]], [[3tc5]] – hPin1 PPIase domain (mutant) + inhibitor<BR />
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**[[4tns]] – hPin1 PPIase domain (mutant) + retinoic acid<BR />
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**[[3kab]], [[3kad]], [[3kaf]], [[3kag]], [[3kah]], [[3kai]], [[3kce]], [[3odk]], [[2xp3]], [[2xp4]], [[2xp5]], [[2xp6]], [[2xp7]], [[2xp8]], [[2xp9]], [[2xpa]], [[2xpb]], [[3oob]], [[3ntp]], [[3tcz]], [[3tdb]], [[4qib]], [[4tyo]] – hPin1 (mutant) + inhibitor<BR />
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**[[4u84]], [[4u85]], [[4u86]] – hPin1 + inhibitor<BR />
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**[[3wh0]] – hPin1 (mutant) + crown ether<BR />
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**[[3oob]] – hPin1 (mutant) + dexamethasone phosphate<BR />
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**[[1c5f]] – Pin1 cyclophilin-like domain + cyclosporine A – ''Brugia malayi'' <BR />
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*PPIase Pin4 (Parvulin 14)
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**[[3ui4]], [[3ui5]] – hPin4 <BR />
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**[[3ui6]] – hPin4 + dithiane diol <BR />
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**[[1eq3]] – hPin4 PPIase domain - NMR<BR />
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*PPIase PinA
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**[[2m1i]], [[2rqs]] – PinA – ''Cenarchaeum symbiosum'' - NMR<BR />
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*PPIase Cyp7
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**[[5jhe]] – PPIase – yeast <BR />
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*PPIase Mip
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**[[1fd9]] – LpMip – ''Legionella pneumophila''<BR />
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**[[2y78]] – BpMip <BR />
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**[[2uz5]] – LpMip FKBP domain - NMR<BR />
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**[[2vcd]] – LpMip FKBP domain + rapamycin - NMR<BR />
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**[[1jvw]] – Mip – ''Trypanosoma cruzi''<BR />
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*PPIase SlyD
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**[[2k8i]], [[2kfw]] – EcSlyD - NMR<BR />
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**[[2kr7]] – FKBP SlyD – NMR - ''Helicobacter pylori''<br />
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**[[3cgm]], [[3cgn]] – TtSlyD – ''Themus thermophilus''<BR />
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**[[3luo]] – TtSlyD + peptide<BR />
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**[[4odk]] – TtSlyD + RNAse T1 peptide<BR />
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**[[4odl]], [[4odm]], [[4odn]], [[4odp]] – TtSlyD + RPS2 peptide<BR />
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**[[4odq]] – TtSlyD + RPS3 peptide<BR />
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**[[4odo]] – TtSlyD + FK506<BR />
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*PPIase SlpA
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**[[4dt4]] – EcSlpA <BR />
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**[[2m2a]] – EcSlpA - NMR<BR />
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*PPIase 3 see [[Cyclophilin]]-3<br />
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*PPIase 5 see [[Cyclophilin]]-5<br />
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*PPIase 38 see [[Cyclophilin]]-38<br />
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*PPIase A see [[Cyclophilin]]-A<br />
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*PPIase B see [[Cyclophilin]]-B<br />
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*PPIase C see [[Cyclophilin]]-C<br />
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*PPIase D see [[Cyclophilin]]-D<br />
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*PPIase E see [[Cyclophilin]]-E<br />
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*PPIase F see [[Cyclophilin]]-F<br />
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*PPIase G see [[Cyclophilin]]-G<br />
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*PPIase FKBP see [[FK506 binding protein]]<br />
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}}
 
[[Category:Topic Page]]
[[Category:Topic Page]]
== References ==
== References ==
<references/>
<references/>

Current revision

Human PPIase (green) complex with phosphoserine containing peptide (magenta) (PDB code 1f8a).

Drag the structure with the mouse to rotate

References

  1. ↑ Guito J, Gavina A, Palmeri D, Lukac DM. The cellular peptidyl-prolyl cis/trans isomerase Pin1 regulates reactivation of Kaposi's sarcoma-associated herpesvirus from latency. J Virol. 2014 Jan;88(1):547-58. doi: 10.1128/JVI.02877-13. Epub 2013 Oct 30. PMID:24173213 doi:http://dx.doi.org/10.1128/JVI.02877-13
  2. ↑ Fischer G, Bang H, Ludwig B, Mann K, Hacker J. Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity. Mol Microbiol. 1992 May;6(10):1375-83. PMID:1379319
  3. ↑ Quistgaard EM, Nordlund P, Low C. High-resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA. FASEB J. 2012 Jun 26. PMID:22735173 doi:10.1096/fj.12-208397
  4. ↑ McClements L, Annett S, Yakkundi A, Robson T. The Role of Peptidyl Prolyl Isomerases in Aging and Vascular Diseases. Curr Mol Pharmacol. 2015;9(2):165-79. PMID:25986561
  5. ↑ Westerman ST. Tasting instilled otologic drops is not a reliable test of eustachian tube function. Arch Otolaryngol Head Neck Surg. 2000 Aug;126(8):1042. PMID:10922246

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