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7zdn
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7zdn is ON HOLD Authors: Silva, D.O., Graedler, U., Bandeiras, T.M. Description: Human Cyclophilin D in complex with fragment [[Category: Unrelease...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Human Cyclophilin D in complex with fragment== | |
| - | + | <StructureSection load='7zdn' size='340' side='right'caption='[[7zdn]], [[Resolution|resolution]] 1.55Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7zdn]] is a 2 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=7ZDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZDN FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IU0:(1~{R},9~{R},10~{S})-12-oxa-8-azatricyclo[7.3.1.0^{2,7}]trideca-2(7),3,5-trien-10-ol'>IU0</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zdn OCA], [https://pdbe.org/7zdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zdn RCSB], [https://www.ebi.ac.uk/pdbsum/7zdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zdn ProSAT]</span></td></tr> |
| - | [[Category: Bandeiras | + | </table> |
| - | [[Category: Silva | + | == Function == |
| + | [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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bandeiras TM]] | ||
| + | [[Category: Graedler U]] | ||
| + | [[Category: Silva DO]] | ||
Current revision
Human Cyclophilin D in complex with fragment
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