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==Crystal structure of cyclophilin D in complex with CsA analogue, JW47.==
==Crystal structure of cyclophilin D in complex with CsA analogue, JW47.==
<StructureSection load='5a0e' size='340' side='right' caption='[[5a0e]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
<StructureSection load='5a0e' size='340' side='right'caption='[[5a0e]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5a0e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A0E FirstGlance]. <br>
<table><tr><td colspan='2'>[[5a0e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cylindrocarpon_lucidum Cylindrocarpon lucidum] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0E FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=AUX:4-METHYL-4-[8-QUINOLINIUM-4-ENE]-4,N-METHYL-THREONINE'>AUX</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=AUX:4-METHYL-4-[8-QUINOLINIUM-4-ENE]-4,N-METHYL-THREONINE'>AUX</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0e OCA], [http://pdbe.org/5a0e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a0e RCSB], [http://www.ebi.ac.uk/pdbsum/5a0e PDBsum]</span></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=5a0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0e OCA], [https://pdbe.org/5a0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0e RCSB], [https://www.ebi.ac.uk/pdbsum/5a0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>
[https://www.uniprot.org/uniprot/PPIF_HUMAN PPIF_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.<ref>PMID:19228691</ref> <ref>PMID:22726440</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5a0e" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5a0e" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Peptidylprolyl isomerase]]
[[Category: Cylindrocarpon lucidum]]
[[Category: Baker, D]]
[[Category: Homo sapiens]]
[[Category: Chan, A W.E]]
[[Category: Large Structures]]
[[Category: Coker, A R]]
[[Category: Baker D]]
[[Category: Duchen, M]]
[[Category: Chan AWE]]
[[Category: Hilditch, L]]
[[Category: Coker AR]]
[[Category: Hill, J]]
[[Category: Duchen M]]
[[Category: Kip, M]]
[[Category: Hilditch L]]
[[Category: Lenneras, F]]
[[Category: Hill J]]
[[Category: Pryce, G]]
[[Category: Kip M]]
[[Category: Puentes, F]]
[[Category: Lenneras F]]
[[Category: Selwood, D L]]
[[Category: Pryce G]]
[[Category: Shi, X]]
[[Category: Puentes F]]
[[Category: Simone, M]]
[[Category: Selwood DL]]
[[Category: Szabadkai, G]]
[[Category: Shi X]]
[[Category: Towers, G]]
[[Category: Simone M]]
[[Category: Walker, P]]
[[Category: Szabadkai G]]
[[Category: Warne, J]]
[[Category: Towers G]]
[[Category: Csa]]
[[Category: Walker P]]
[[Category: Cyclophilin]]
[[Category: Warne J]]
[[Category: Cyclophilin d]]
[[Category: Cyclosporin some]]
[[Category: Cyp d]]
[[Category: Isomerase]]
[[Category: Jw47]]
[[Category: Mitochondrial permeability transition pore]]
[[Category: Peptidylprolyl cis-trans isomerase]]
[[Category: Ppif]]
[[Category: Ptp]]
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