3rd9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rd9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RD9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3rd9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RD9 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSY:3-(3-METHYL-5-OXO-4,5-DIHYDRO-1H-PYRAZOL-1-YL)BENZENESULFONAMIDE'>MSY</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSY:3-(3-METHYL-5-OXO-4,5-DIHYDRO-1H-PYRAZOL-1-YL)BENZENESULFONAMIDE'>MSY</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r49|3r49]], [[3r4g|3r4g]], [[3r54|3r54]], [[3r56|3r56]], [[3r57|3r57]], [[3r59|3r59]], [[3rcf|3rcf]], [[3rcg|3rcg]], [[3rci|3rci]], [[3rck|3rck]], [[3rcl|3rcl]], [[3rda|3rda]], [[3rdb|3rdb]], [[3rdc|3rdc]], [[3rdd|3rdd]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r49|3r49]], [[3r4g|3r4g]], [[3r54|3r54]], [[3r56|3r56]], [[3r57|3r57]], [[3r59|3r59]], [[3rcf|3rcf]], [[3rcg|3rcg]], [[3rci|3rci]], [[3rck|3rck]], [[3rcl|3rcl]], [[3rda|3rda]], [[3rdb|3rdb]], [[3rdc|3rdc]], [[3rdd|3rdd]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIF, CYP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIF, CYP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rd9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rd9 RCSB], [http://www.ebi.ac.uk/pdbsum/3rd9 PDBsum]</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=3rd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rd9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rd9 RCSB], [http://www.ebi.ac.uk/pdbsum/3rd9 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Cyclophilin|Cyclophilin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | [[Category: Ahmed-Belkacem, H | + | [[Category: Ahmed-Belkacem, H]] |
| - | [[Category: Bessin, Y | + | [[Category: Bessin, Y]] |
| - | [[Category: Colliandre, L | + | [[Category: Colliandre, L]] |
| - | [[Category: Guichou, J F | + | [[Category: Guichou, J F]] |
| - | [[Category: Pawlotsky, J M | + | [[Category: Pawlotsky, J M]] |
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
Revision as of 16:56, 25 December 2014
Human Cyclophilin D Complexed with a Fragment
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