5ccs: Difference between revisions

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<StructureSection load='5ccs' size='340' side='right'caption='[[5ccs]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5ccs' size='340' side='right'caption='[[5ccs]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ccs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCS FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ccs]] 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=5CCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C4Y:1-(4-AMINOBENZYL)-3-{2-OXO-2-[(2R)-2-PHENYLPYRROLIDIN-1-YL]ETHYL}UREA'>C4Y</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C4Y:1-(4-AMINOBENZYL)-3-{2-OXO-2-[(2R)-2-PHENYLPYRROLIDIN-1-YL]ETHYL}UREA'>C4Y</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'>[https://proteopedia.org/fgij/fg.htm?mol=5ccs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccs OCA], [https://pdbe.org/5ccs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccs RCSB], [https://www.ebi.ac.uk/pdbsum/5ccs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccs ProSAT]</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=5ccs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccs OCA], [http://pdbe.org/5ccs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ccs RCSB], [http://www.ebi.ac.uk/pdbsum/5ccs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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>  


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Awais M]]
[[Category: Awais, M]]
[[Category: Berry N]]
[[Category: Berry, N]]
[[Category: Gibson RP]]
[[Category: Gibson, R P]]
[[Category: Javed A]]
[[Category: Javed, A]]
[[Category: Kershaw N]]
[[Category: Kershaw, N]]
[[Category: Latawiec D]]
[[Category: Latawiec, D]]
[[Category: Lian LY]]
[[Category: Lian, L Y]]
[[Category: O'Neill P]]
[[Category: Neill, P O]]
[[Category: Pandalaneni S]]
[[Category: Pandalaneni, S]]
[[Category: Shore E]]
[[Category: Shore, E]]
[[Category: Sutton R]]
[[Category: Sutton, R]]
[[Category: Wen L]]
[[Category: Wen, L]]
[[Category: Complex]]
[[Category: Cyclophilin]]
[[Category: Inhibitor]]
[[Category: Isomerase]]

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