3rdc - Revision history

OCA at 12:19, 14 March 2024

2024-03-14T12:19:27Z

← Older revision		Revision as of 12:19, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3rdc' size='340' side='right'caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='3rdc' size='340' side='right'caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rdc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDC FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EA4:ETHYL+N~~-~~[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</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]] 1.94Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; max-height: 3em;'>[[3r49\|3r49]], [[3r4g\|3r4g]], [[3r54\|3r54]], [[3r56\|3r56]], [[3r57\|3r57]], [[3r59\|3r59]], [[3rcf\|3rcf]], [[3rcg\|3rcg]], [[3rci\|3rci]], [[3rck\|3rck]], [[3rcl\|3rcl]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[3rdd\|3rdd]]</div></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EA4:ETHYL+N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</scene></td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PPIF, CYP3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=9606 HUMAN])</td></tr>~~
	~~<tr id='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number~~ [~~https://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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [https://pdbe.org/3rdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [https://www.ebi.ac.uk/pdbsum/3rdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdc ProSAT]</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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [https://pdbe.org/3rdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [https://www.ebi.ac.uk/pdbsum/3rdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdc ProSAT]</span></td></tr>
	</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>		[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 ==~~
	X-ray crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-ray diffraction is performed directly `in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-ray crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.

	Combining `dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.,Gelin M, Delfosse V, Allemand F, Hoh F, Sallaz-Damaz Y, Pirocchi M, Bourguet W, Ferrer JL, Labesse G, Guichou JF Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1777-87. doi:, 10.1107/S1399004715010342. Epub 2015 Jul 31. PMID:26249358<ref>PMID:26249358</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3rdc" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==
Line 28:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[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 JF]]
	[[Category: Guichou~~, J F~~]]		[[Category: Pawlotsky JM]]
	[[Category: Pawlotsky~~, J M]]~~
	~~[[Category: Beta barrel]]~~
	~~[[Category: Inhibitor]]~~
	~~[[Category: Isomerase-isomerase inhibitor complex]]~~
	~~[[Category: Mitochondria]]~~
	~~[[Category: Prolyl cis/trans isomerase~~]]

OCA at 05:58, 15 June 2022

2022-06-15T05:58:50Z

← Older revision		Revision as of 05:58, 15 June 2022
Line 1:		Line 1:

	==Human Cyclophilin D Complexed with an Inhibitor==		==Human Cyclophilin D Complexed with an Inhibitor==
	<StructureSection load='3rdc' size='340' side='right' caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='3rdc' size='340' side='right'caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3RDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rdc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDC 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>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EA4:ETHYL+N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</scene></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]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[3rdd\|3rdd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r49\|3r49]], [[3r4g\|3r4g]], [[3r54\|3r54]], [[3r56\|3r56]], [[3r57\|3r57]], [[3r59\|3r59]], [[3rcf\|3rcf]], [[3rcg\|3rcg]], [[3rci\|3rci]], [[3rck\|3rck]], [[3rcl\|3rcl]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[3rdd\|3rdd]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIF, CYP3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [~~http~~://pdbe.org/3rdc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rdc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdc ProSAT]</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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [https://pdbe.org/3rdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [https://www.ebi.ac.uk/pdbsum/3rdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdc 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
	*[[Cyclophilin\|Cyclophilin]]		*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Ahmed-Belkacem, H]]		[[Category: Ahmed-Belkacem, H]]

OCA at 09:49, 19 October 2016

2016-10-19T09:49:37Z

← Older revision		Revision as of 09:49, 19 October 2016
Line 1:		Line 1:

	==Human Cyclophilin D Complexed with an Inhibitor==		==Human Cyclophilin D Complexed with an Inhibitor==
	<StructureSection load='3rdc' size='340' side='right' caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='3rdc' size='340' side='right' caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>
Line 7:		Line 8:
	<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='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='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='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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc 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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://pdbe.org/3rdc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdc 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>		[[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>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			X-ray crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-ray diffraction is performed directly `in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-ray crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.

			Combining `dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.,Gelin M, Delfosse V, Allemand F, Hoh F, Sallaz-Damaz Y, Pirocchi M, Bourguet W, Ferrer JL, Labesse G, Guichou JF Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1777-87. doi:, 10.1107/S1399004715010342. Epub 2015 Jul 31. PMID:26249358<ref>PMID:26249358</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 3rdc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 08:25, 12 August 2015

2015-08-12T08:25:17Z

← Older revision		Revision as of 08:25, 12 August 2015
Line 2:		Line 2:
	<StructureSection load='3rdc' size='340' side='right' caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='3rdc' size='340' side='right' caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDC 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>		</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='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]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[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]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[3rdd\|3rdd]]</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 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='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='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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc 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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc PDBsum]</span></td></tr>
Line 18:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Ahmed-Belkacem, H]]		[[Category: Ahmed-Belkacem, H]]

OCA at 16:22, 24 December 2014

2014-12-24T16:22:32Z

← Older revision		Revision as of 16:22, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDC FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EA4:ETHYL+N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</scene><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><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]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[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]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc 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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc 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]]

OCA at 04:50, 5 June 2014

2014-06-05T04:50:45Z

← Older revision		Revision as of 04:50, 5 June 2014
Line 1:		Line 1:
	~~[[Image:3rdc.jpg\|left\|200px]]~~		==Human Cyclophilin D Complexed with an Inhibitor==
			<StructureSection load='3rdc' size='340' side='right' caption='[[3rdc]], [[Resolution\|resolution]] 1.94Å' scene=''>
	~~<!--~~		== Structural highlights ==
	~~The line below this paragraph, containing "STRUCTURE_3rdc", creates the "Structure Box" on the page.~~		<table><tr><td colspan='2'>[[3rdc]] 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=3RDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDC FirstGlance]. <br>
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EA4:ETHYL+N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE'>EA4</scene><br>
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~		<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]], [[3rd9\|3rd9]], [[3rda\|3rda]], [[3rdb\|3rdb]], [[3rdd\|3rdd]]</td></tr>
	~~or leave the SCENE parameter empty for the default display.~~		<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><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>
	~~{{STRUCTURE_3rdc\| PDB=3rdc \| SCENE= }}~~		<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=3rdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdc RCSB], [http://www.ebi.ac.uk/pdbsum/3rdc PDBsum]</span></td></tr>
			<table>
	===Human Cyclophilin D Complexed with an Inhibitor===		__TOC__
			</StructureSection>

	==~~About this Structure~~==
	[[3rdc]] 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=3RDC OCA].
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]

OCA at 07:44, 21 March 2012

2012-03-21T07:44:49Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3rdc.jpg|left|200px]]
-The entry 3rdc is ON HOLD  until Paper Publication
+<!--
-Authors: Colliandre, L., Ahmed-Belkacem, H., Bessin, Y., Pawlotsky, J.M., Guichou, J.F.
+===Human Cyclophilin D Complexed with an Inhibitor===
-Description: Human Cyclophilin D Complexed with an Inhibitor

OCA: Protected "3rdc" [edit=sysop:move=sysop]

2011-04-13T04:58:49Z

Protected "3rdc" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:58, 13 April 2011
(No difference)

OCA: New page: '''Unreleased structure''' The entry 3rdc is ON HOLD until Paper Publication Authors: Colliandre, L., Ahmed-Belkacem, H., Bessin, Y., Pawlotsky, J.M., Guichou, J.F. Description: Human ...

2011-04-13T04:58:48Z

New page: '''Unreleased structure''' The entry 3rdc is ON HOLD until Paper Publication Authors: Colliandre, L., Ahmed-Belkacem, H., Bessin, Y., Pawlotsky, J.M., Guichou, J.F. Description: Human ...

New page

'''Unreleased structure'''

The entry 3rdc is ON HOLD until Paper Publication

Authors: Colliandre, L., Ahmed-Belkacem, H., Bessin, Y., Pawlotsky, J.M., Guichou, J.F.

Description: Human Cyclophilin D Complexed with an Inhibitor