5cbu

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'''Unreleased structure'''
 
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The entry 5cbu is ON HOLD until Paper Publication
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==Human Cyclophilin D Complexed with Inhibitor.==
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<StructureSection load='5cbu' size='340' side='right'caption='[[5cbu]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5cbu]] 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=5CBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CBU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4ZM:ETHYL+N-{[3-(PYRIDIN-4-YL)BENZYL]CARBAMOYL}GLYCINATE'>4ZM</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbu OCA], [https://pdbe.org/5cbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cbu RCSB], [https://www.ebi.ac.uk/pdbsum/5cbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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Authors:
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==See Also==
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Awais M]]
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[[Category: Berry N]]
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[[Category: Gibson RP]]
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[[Category: Javed A]]
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[[Category: Kershaw N]]
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[[Category: Latawiec D]]
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[[Category: Lian LY]]
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[[Category: O'Neill P]]
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[[Category: Pandalaneni S]]
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[[Category: Shore E]]
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[[Category: Sutton R]]
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[[Category: Wen L]]

Current revision

Human Cyclophilin D Complexed with Inhibitor.

PDB ID 5cbu

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