View source for 4j5e


==Human Cyclophilin D Complexed with an Inhibitor==
<StructureSection load='4j5e' size='340' side='right' caption='[[4j5e]], [[Resolution|resolution]] 0.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4j5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J5E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7B7:1-(4-AMINOBENZYL)-3-{2-[(2R)-2-(2-METHOXYPHENYL)PYRROLIDIN-1-YL]-2-OXOETHYL}UREA'>7B7</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j58|4j58]], [[4j59|4j59]], [[4j5a|4j5a]], [[4j5b|4j5b]], [[4j5c|4j5c]], [[4j5d|4j5d]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP3, PPIF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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=4j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5e OCA], [http://pdbe.org/4j5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j5e RCSB], [http://www.ebi.ac.uk/pdbsum/4j5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5e ProSAT]</span></td></tr>
</table>
== 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>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Bessin, Y]]
[[Category: Colliandre, L]]
[[Category: Gelin, M]]
[[Category: Guichou, J F]]
[[Category: Isomerase-isomerase inhibitor complex]]