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3rdb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human Cyclophilin D Complexed with a Fragment== | |
| + | <StructureSection load='3rdb' size='340' side='right'caption='[[3rdb]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3rdb]] 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=3RDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDB 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> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5MZ:3-[5-(CHLOROMETHYL)-1,2,4-OXADIAZOL-3-YL]ANILINE'>5MZ</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdb OCA], [https://pdbe.org/3rdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdb RCSB], [https://www.ebi.ac.uk/pdbsum/3rdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| - | + | ==See Also== | |
| - | + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ahmed-Belkacem H]] | ||
| + | [[Category: Bessin Y]] | ||
| + | [[Category: Colliandre L]] | ||
| + | [[Category: Guichou JF]] | ||
| + | [[Category: Pawlotsky JM]] | ||
Current revision
Human Cyclophilin D Complexed with a Fragment
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