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4j58

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{{STRUCTURE_4j58| PDB=4j58 | SCENE= }}
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==Human Cyclophilin D Complexed with an Inhibitor==
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===Human Cyclophilin D Complexed with an Inhibitor===
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<StructureSection load='4j58' size='340' side='right' caption='[[4j58]], [[Resolution|resolution]] 1.28&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4j58]] 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=4J58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J58 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=53Z:1-(4-AMINOBENZYL)-3-[2-OXO-2-(PYRROLIDIN-1-YL)ETHYL]UREA'>53Z</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j59|4j59]], [[4j5a|4j5a]], [[4j5b|4j5b]], [[4j5c|4j5c]], [[4j5d|4j5d]], [[4j5e|4j5e]]</td></tr>
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<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>
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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=4j58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j58 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j58 RCSB], [http://www.ebi.ac.uk/pdbsum/4j58 PDBsum]</span></td></tr>
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</table>
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==Function==
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==See Also==
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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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*[[Cyclophilin|Cyclophilin]]
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__TOC__
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==About this Structure==
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</StructureSection>
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[[4j58]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J58 OCA].
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[[Category: Human]]
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
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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, J F]]
[[Category: Isomerase-isomerase inhibitor complex]]
[[Category: Isomerase-isomerase inhibitor complex]]

Revision as of 18:39, 21 December 2014

Human Cyclophilin D Complexed with an Inhibitor

4j58, resolution 1.28Å

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