4zsc: Difference between revisions

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-'''Unreleased structure'''
+==Human Cyclophilin D Complexed with an Inhibitor at room temperature==
+<StructureSection load='4zsc' size='340' side='right' caption='[[4zsc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-The entry 4zsc is ON HOLD
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4zsc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZSC FirstGlance]. <br>
-Authors: Gelin, M., Delfosse, V., Allemand, F., Hoh, F., Sallaz-Damaz, Y., Pirocchi, M., Bourguet, W., Ferrer, J.-L., Labesse, G., Guichou, J.-F.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EA4:ETHYL+N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rdc|3rdc]]</td></tr>
-Description: Human Cyclophilin D Complexed with an Inhibitor at room temperature
+<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>
-[[Category: Unreleased Structures]]
+<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=4zsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zsc RCSB], [http://www.ebi.ac.uk/pdbsum/4zsc PDBsum]</span></td></tr>
-[[Category: Guichou, J.-F]]
+</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: Peptidylprolyl isomerase]]
+[[Category: Allemand, F]]
+[[Category: Bourguet, W]]
 [[Category: Delfosse, V]]
-[[Category: Allemand, F]]
+[[Category: Ferrer, J L]]
-[[Category: Labesse, G]]
-[[Category: Sallaz-Damaz, Y]]
 [[Category: Gelin, M]]
-[[Category: Bourguet, W]]
+[[Category: Guichou, J F]]
-[[Category: Ferrer, J.-L]]
 [[Category: Hoh, F]]
+[[Category: Labesse, G]]
 [[Category: Pirocchi, M]]
+[[Category: Sallaz-Damaz, Y]]
+[[Category: Isomerase]]
+[[Category: Isomerase inhibitor complex]]