5ccq: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ccq is ON HOLD
+==Human Cyclophilin D Complexed with Inhibitor==
+<StructureSection load='5ccq' size='340' side='right'caption='[[5ccq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ccq]] 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=5CCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCQ 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]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=502:ETHYL+N-{[(2-AMINOPYRIDIN-4-YL)METHYL]CARBAMOYL}GLYCINATE'>502</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=5ccq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccq OCA], [https://pdbe.org/5ccq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccq RCSB], [https://www.ebi.ac.uk/pdbsum/5ccq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccq 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>
-Authors: Gibson, R.P., Shore, E., Kershaw, N., Awais, M., Javed, A., Latawiec, D., Pandalaneni, S., Wen, L., Berry, N., O'Neill, P., Sutton, R., Lian, L.Y.
+==See Also==
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-Description:
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Javed, A]]
+__TOC__
-[[Category: Kershaw, N]]
+</StructureSection>
-[[Category: Sutton, R]]
+[[Category: Homo sapiens]]
-[[Category: Pandalaneni, S]]
+[[Category: Large Structures]]
-[[Category: Berry, N]]
+[[Category: Awais M]]
-[[Category: Awais, M]]
+[[Category: Berry N]]
-[[Category: O'Neill, P]]
+[[Category: Gibson RP]]
-[[Category: Lian, L.Y]]
+[[Category: Javed A]]
-[[Category: Wen, L]]
+[[Category: Kershaw N]]
-[[Category: Latawiec, D]]
+[[Category: Latawiec D]]
-[[Category: Gibson, R.P]]
+[[Category: Lian LY]]
-[[Category: Shore, E]]
+[[Category: O'Neill P]]
+[[Category: Pandalaneni S]]
+[[Category: Shore E]]
+[[Category: Sutton R]]
+[[Category: Wen L]]