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4j59

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==Human Cyclophilin D Complexed with an Inhibitor==
==Human Cyclophilin D Complexed with an Inhibitor==
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<StructureSection load='4j59' size='340' side='right' caption='[[4j59]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
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<StructureSection load='4j59' size='340' side='right'caption='[[4j59]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4j59]] 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=4J59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J59 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4j59]] is a 1 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=4J59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J59 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=671:1-(4-AMINOBENZYL)-3-{2-[(2R)-2-(NAPHTHALEN-1-YL)PYRROLIDIN-1-YL]-2-OXOETHYL}UREA'>671</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j58|4j58]], [[4j5a|4j5a]], [[4j5b|4j5b]], [[4j5c|4j5c]], [[4j5d|4j5d]], [[4j5e|4j5e]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=671:1-(4-AMINOBENZYL)-3-{2-[(2R)-2-(NAPHTHALEN-1-YL)PYRROLIDIN-1-YL]-2-OXOETHYL}UREA'>671</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ppif, cyp3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j59 OCA], [https://pdbe.org/4j59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j59 RCSB], [https://www.ebi.ac.uk/pdbsum/4j59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j59 ProSAT]</span></td></tr>
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<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>
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<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=4j59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j59 RCSB], [http://www.ebi.ac.uk/pdbsum/4j59 PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[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>
==See Also==
==See Also==
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*[[Cyclophilin|Cyclophilin]]
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Bessin, Y]]
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[[Category: Bessin Y]]
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[[Category: Colliandre, L]]
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[[Category: Colliandre L]]
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[[Category: Gelin, M]]
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[[Category: Gelin M]]
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[[Category: Guichou, J F]]
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[[Category: Guichou JF]]
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[[Category: Isomerase-isomerase inhibitor complex]]
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Current revision

Human Cyclophilin D Complexed with an Inhibitor

PDB ID 4j59

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