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4xnc
From Proteopedia
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| - | ''' | + | ==Crystal structure at room temperature of cyclophilin D in complex with an inhibitor== |
| - | + | <StructureSection load='4xnc' size='340' side='right' caption='[[4xnc]], [[Resolution|resolution]] 2.23Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4xnc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XNC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EA4:ETHYL+N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</scene></td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xnc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xnc RCSB], [http://www.ebi.ac.uk/pdbsum/4xnc PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[Category: | + | == Function == |
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Allemand, F]] | [[Category: Allemand, F]] | ||
| - | [[Category: Labesse, G]] | ||
[[Category: Gelin, M]] | [[Category: Gelin, M]] | ||
| + | [[Category: Guichou, J F]] | ||
| + | [[Category: Labesse, G]] | ||
| + | [[Category: Inhibitor isomerase fragment based drug design]] | ||
| + | [[Category: Isomerase]] | ||
Revision as of 14:49, 12 August 2015
Crystal structure at room temperature of cyclophilin D in complex with an inhibitor
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