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3rcl

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==Human Cyclophilin D Complexed with a Fragment==
==Human Cyclophilin D Complexed with a Fragment==
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<StructureSection load='3rcl' size='340' side='right' caption='[[3rcl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='3rcl' size='340' side='right'caption='[[3rcl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rcl]] 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=3RCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RCL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rcl]] 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=3RCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RCL 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=5AO:3-(1,3-OXAZOL-5-YL)ANILINE'>5AO</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</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]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r49|3r49]], [[3r4g|3r4g]], [[3r54|3r54]], [[3r56|3r56]], [[3r57|3r57]], [[3r59|3r59]], [[3rcf|3rcf]], [[3rcg|3rcg]], [[3rci|3rci]], [[3rck|3rck]], [[3rd9|3rd9]], [[3rda|3rda]], [[3rdb|3rdb]], [[3rdc|3rdc]], [[3rdd|3rdd]]</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=5AO:3-(1,3-OXAZOL-5-YL)ANILINE'>5AO</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</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=3rcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rcl OCA], [https://pdbe.org/3rcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rcl RCSB], [https://www.ebi.ac.uk/pdbsum/3rcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rcl 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=3rcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rcl OCA], [http://pdbe.org/3rcl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rcl RCSB], [http://www.ebi.ac.uk/pdbsum/3rcl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rcl ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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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]]
== References ==
== References ==
<references/>
<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: Ahmed-Belkacem, H]]
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[[Category: Ahmed-Belkacem H]]
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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: Guichou, J F]]
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[[Category: Guichou JF]]
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[[Category: Pawlotsky, J M]]
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[[Category: Pawlotsky JM]]
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[[Category: Beta barrel]]
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[[Category: Inhibitor]]
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[[Category: Isomerase-isomerase inhibitor complex]]
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[[Category: Mitochondria]]
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[[Category: Prolyl cis/trans isomerase]]
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Current revision

Human Cyclophilin D Complexed with a Fragment

PDB ID 3rcl

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