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4o8h
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4o8h is ON HOLD Authors: Lovell, Scott, Valasani, Koteswara Rao, Battaile, Kevin P., Wang, Chunyu, Yan, Shirley ShiDu Description: 0.85A resolution...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==0.85A resolution structure of PEG 400 Bound Cyclophilin D== | |
| + | <StructureSection load='4o8h' size='340' side='right'caption='[[4o8h]], [[Resolution|resolution]] 0.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4o8h]] 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=4O8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O8H 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]] 0.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4o8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8h OCA], [https://pdbe.org/4o8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o8h RCSB], [https://www.ebi.ac.uk/pdbsum/4o8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8h 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4o8h" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Battaile KP]] | ||
| + | [[Category: Lovell S]] | ||
| + | [[Category: Valasani KR]] | ||
| + | [[Category: Wang C]] | ||
| + | [[Category: Yan SS]] | ||
Current revision
0.85A resolution structure of PEG 400 Bound Cyclophilin D
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Categories: Homo sapiens | Large Structures | Battaile KP | Lovell S | Valasani KR | Wang C | Yan SS
