4o8i

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(New page: '''Unreleased structure''' The entry 4o8i is ON HOLD Authors: Lovell, Scott, Valasani, Koteswara Rao, Battaile, Kevin P., Wang, Chunyu, Yan, Shirley ShiDu Description: 1.45A resolution...)
Current revision (17:08, 20 September 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4o8i is ON HOLD
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==1.45A resolution structure of PEG 400 Bound Cyclophilin D==
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<StructureSection load='4o8i' size='340' side='right'caption='[[4o8i]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4o8i]] 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=4O8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O8I 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]] 1.45&#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=1PE:PENTAETHYLENE+GLYCOL'>1PE</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=4o8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8i OCA], [https://pdbe.org/4o8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o8i RCSB], [https://www.ebi.ac.uk/pdbsum/4o8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8i 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclophilin D (CypD) is a key mitochondrial target for amyloid-beta-induced mitochondrial and synaptic dysfunction and is considered a potential drug target for Alzheimer's disease. The high-resolution crystal structures of primitive orthorhombic (CypD-o) and primitive tetragonal (CypD-t) forms have been determined to 1.45 and 0.85 A resolution, respectively, and are nearly identical structurally. Although an isomorphous structure of CypD-t has previously been reported, the structure reported here was determined at atomic resolution, while CypD-o represents a new crystal form for this protein. In addition, each crystal form contains a PEG 400 molecule bound to the same region along with a second PEG 400 site in CypD-t which occupies the cyclosporine A inhibitor binding site of CypD. Highly precise structural information for CypD should be extremely useful for discerning the detailed interaction of small molecules, particularly drugs and/or inhibitors, bound to CypD. The 0.85 A resolution structure of CypD-t is the highest to date for any CypD structure.
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Authors: Lovell, Scott, Valasani, Koteswara Rao, Battaile, Kevin P., Wang, Chunyu, Yan, Shirley ShiDu
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High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.,Valasani KR, Carlson EA, Battaile KP, Bisson A, Wang C, Lovell S, ShiDu Yan S Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):717-22. doi:, 10.1107/S2053230X14009480. Epub 2014 May 24. PMID:24915078<ref>PMID:24915078</ref>
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Description: 1.45A resolution structure of PEG 400 Bound Cyclophilin D
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4o8i" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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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: Battaile KP]]
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[[Category: Lovell S]]
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[[Category: Valasani KR]]
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[[Category: Wang C]]
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[[Category: Yan SS]]

Current revision

1.45A resolution structure of PEG 400 Bound Cyclophilin D

PDB ID 4o8i

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