4o8h: Difference between revisions
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==0.85A resolution structure of PEG 400 Bound Cyclophilin D== | ==0.85A resolution structure of PEG 400 Bound Cyclophilin D== | ||
<StructureSection load='4o8h' size='340' side='right' caption='[[4o8h]], [[Resolution|resolution]] 0.85Å' scene=''> | <StructureSection load='4o8h' size='340' side='right'caption='[[4o8h]], [[Resolution|resolution]] 0.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4o8h]] is a 1 chain structure with sequence from [ | <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=' | </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=' | <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> | ||
<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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4o8h" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4o8h" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Battaile | [[Category: Battaile KP]] | ||
[[Category: Lovell | [[Category: Lovell S]] | ||
[[Category: Valasani | [[Category: Valasani KR]] | ||
[[Category: Wang | [[Category: Wang C]] | ||
[[Category: Yan | [[Category: Yan SS]] | ||