4zsd

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==Human Cyclophilin D Complexed with an Inhibitor at room temperature==
==Human Cyclophilin D Complexed with an Inhibitor at room temperature==
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<StructureSection load='4zsd' size='340' side='right' caption='[[4zsd]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='4zsd' size='340' side='right'caption='[[4zsd]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4zsd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZSD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZSD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4zsd]] 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=4ZSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZSD 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=7I6:1-(4-AMINOBENZYL)-3-[(2S)-4-(METHYLSULFANYL)-1-{(2R)-2-[2-(METHYLSULFANYL)PHENYL]PYRROLIDIN-1-YL}-1-OXOBUTAN-2-YL]UREA'>7I6</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]] 1.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5c|4j5c]]</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=7I6:1-(4-AMINOBENZYL)-3-[(2S)-4-(METHYLSULFANYL)-1-{(2R)-2-[2-(METHYLSULFANYL)PHENYL]PYRROLIDIN-1-YL}-1-OXOBUTAN-2-YL]UREA'>7I6</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4zsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zsd OCA], [https://pdbe.org/4zsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zsd RCSB], [https://www.ebi.ac.uk/pdbsum/4zsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zsd ProSAT]</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=4zsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zsd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zsd RCSB], [http://www.ebi.ac.uk/pdbsum/4zsd PDBsum]</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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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X-ray crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-ray diffraction is performed directly `in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-ray crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.
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Combining `dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.,Gelin M, Delfosse V, Allemand F, Hoh F, Sallaz-Damaz Y, Pirocchi M, Bourguet W, Ferrer JL, Labesse G, Guichou JF Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1777-87. doi:, 10.1107/S1399004715010342. Epub 2015 Jul 31. PMID:26249358<ref>PMID:26249358</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4zsd" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Homo sapiens]]
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[[Category: Allemand, F]]
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[[Category: Large Structures]]
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[[Category: Bourguet, W]]
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[[Category: Allemand F]]
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[[Category: Delfosse, V]]
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[[Category: Bourguet W]]
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[[Category: Ferrer, J L]]
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[[Category: Delfosse V]]
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[[Category: Gelin, M]]
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[[Category: Ferrer J-L]]
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[[Category: Guichou, J F]]
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[[Category: Gelin M]]
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[[Category: Hoh, F]]
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[[Category: Guichou J-F]]
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[[Category: Labesse, G]]
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[[Category: Hoh F]]
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[[Category: Pirocchi, M]]
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[[Category: Labesse G]]
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[[Category: Sallaz-Damaz, Y]]
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[[Category: Pirocchi M]]
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[[Category: Isomerase]]
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[[Category: Sallaz-Damaz Y]]
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[[Category: Isomerase inhibitor complex]]
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Current revision

Human Cyclophilin D Complexed with an Inhibitor at room temperature

PDB ID 4zsd

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