4j5c
From Proteopedia
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==Human Cyclophilin D Complexed with an Inhibitor== | ==Human Cyclophilin D Complexed with an Inhibitor== | ||
| - | <StructureSection load='4j5c' size='340' side='right' caption='[[4j5c]], [[Resolution|resolution]] 1.03Å' scene=''> | + | <StructureSection load='4j5c' size='340' side='right'caption='[[4j5c]], [[Resolution|resolution]] 1.03Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4j5c]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4j5c]] 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=4J5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J5C FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.03Å</td></tr> |
| - | + | <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> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5c OCA], [https://pdbe.org/4j5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j5c RCSB], [https://www.ebi.ac.uk/pdbsum/4j5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5c ProSAT]</span></td></tr> |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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== | ==See Also== | ||
| - | *[[Cyclophilin|Cyclophilin]] | + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bessin | + | [[Category: Bessin Y]] |
| - | [[Category: Colliandre | + | [[Category: Colliandre L]] |
| - | [[Category: Gelin | + | [[Category: Gelin M]] |
| - | [[Category: Guichou | + | [[Category: Guichou JF]] |
| - | + | ||
Current revision
Human Cyclophilin D Complexed with an Inhibitor
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