2ruc - Revision history

OCA at 20:52, 12 April 2023

OCA — Wed, 12 Apr 2023 20:52:58 GMT

←Older revision		Revision as of 20:52, 12 April 2023
Line 1:		Line 1:

	==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==		==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==
-	<StructureSection load='2ruc' size='340' side='right'caption='[[2ruc~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='2ruc' size='340' side='right'caption='[[2ruc]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUC FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rud\|2rud]]</div></td></tr>~~	+	</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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [https://pdbe.org/2ruc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [https://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIN1 ([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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [https://pdbe.org/2ruc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [https://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN]] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>	+	[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Tamari Y]]
-	[[Category: Tamari, Y]]	+	[[Category: Tate S]]
-	[[Category: Tate, S]]	+	[[Category: Tochio N]]
-	[[Category: Tochio, N]]	+	[[Category: Xu N]]
-	[[Category: Xu, N]]	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Ppiase]]~~	+
-	~~[[Category: Protein/cis-trans-isomerase~~]]	+

OCA at 10:36, 7 July 2021

OCA — Wed, 07 Jul 2021 10:36:50 GMT

←Older revision		Revision as of 10:36, 7 July 2021
Line 1:		Line 1:

	==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==		==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==
-	<StructureSection load='2ruc' size='340' side='right' caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='2ruc' size='340' side='right'caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2RUC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUC FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rud\|2rud]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rud\|2rud]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIN1 ([~~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">PIN1 ([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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [~~http~~://pdbe.org/2ruc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc 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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [https://pdbe.org/2ruc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [https://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN]] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>	+	[[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN]] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Peptidyl-prolyl cis-trans isomerase\|Peptidyl-prolyl cis-trans isomerase]]	+	*[[Peptidyl-prolyl cis-trans isomerase 3D structures\|Peptidyl-prolyl cis-trans isomerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Tamari, Y]]		[[Category: Tamari, Y]]

OCA at 08:22, 12 September 2018

OCA — Wed, 12 Sep 2018 08:22:00 GMT

←Older revision		Revision as of 08:22, 12 September 2018
Line 3:		Line 3:
	<StructureSection load='2ruc' size='340' side='right' caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2ruc' size='340' side='right' caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RUC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RUC FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rud\|2rud]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rud\|2rud]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIN1 ([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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://pdbe.org/2ruc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc 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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://pdbe.org/2ruc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc ProSAT]</span></td></tr>
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Tamari, Y]]		[[Category: Tamari, Y]]

OCA at 19:57, 5 August 2016

OCA — Fri, 05 Aug 2016 19:57:21 GMT

←Older revision		Revision as of 19:57, 5 August 2016
Line 1:		Line 1:
		+
	==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==		==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==
	<StructureSection load='2ruc' size='340' side='right' caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2ruc' size='340' side='right' caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rud\|2rud]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rud\|2rud]]</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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc 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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://pdbe.org/2ruc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2ruc" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Peptidyl-prolyl cis-trans isomerase\|Peptidyl-prolyl cis-trans isomerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:29, 25 December 2014

OCA — Thu, 25 Dec 2014 21:29:11 GMT

←Older revision		Revision as of 21:29, 25 December 2014
Line 7:		Line 7:
	<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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc 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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN]] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:35, 17 December 2014

OCA — Wed, 17 Dec 2014 12:35:38 GMT

←Older revision		Revision as of 12:35, 17 December 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion==
		+	<StructureSection load='2ruc' size='340' side='right' caption='[[2ruc]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2ruc]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RUC FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2rud\|2rud]]</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=2ruc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ruc RCSB], [http://www.ebi.ac.uk/pdbsum/2ruc PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Pin1 peptidyl-prolyl isomerase (PPIase) catalyzes specifically the pSer/pThr-Pro motif. The cis-trans isomerization mechanism has been studied by various approaches, including X-ray crystallography, site-directed mutagenesis, and the kinetic isotope effect on isomerization. However, a complete picture of the reaction mechanism remains elusive. On the basis of the X-ray structure of Pin1, residue C113 was proposed to play a nucleophile attacker to catalyze the isomerization. The controversial result that the C113D Pin1 mutant retains the activity, albeit at a reduced level, challenges the importance of C113 as a catalyst. To facilitate our understanding of the Pin1 isomerization process, we compared the structures and dynamics of the wild type with those of the C113D mutant Pin1 PPIase domains (residues 51-163). We found the C113D mutation disturbed the hydrogen bonds between the conserved histidine residues, H59 and H157 ("dual-histidine motif"); H59 imidazole forms a stable hydrogen bond to H157 in the wild type, whereas it has a strong hydrogen bond to D113 with weakened bonding to H157 in the C113D mutant. The C113D mutation unbalanced the hydrogen bonding tug of war for H59 between C113/D113 and H157 and destabilized the catalytic site structure, which eventually resulted in an altered conformation of the basic triad (K63, R68, and R69) that binds to the phosphate group in a substrate. The change in the basic triad structure could explain the severely weakened substrate binding ability of the C113D mutant. Overall, this work demonstrated that C113 plays a role in keeping the catalytic site in an active fold, which has never before been described.

-	The ~~entry 2ruc is ON HOLD until Paper Publication~~	+	The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif.,Xu N, Tochio N, Wang J, Tamari Y, Uewaki J, Utsunomiya-Tate N, Igarashi K, Shiraki T, Kobayashi N, Tate S Biochemistry. 2014 Sep 2;53(34):5568-78. doi: 10.1021/bi5007817. Epub 2014 Aug, 20. PMID:25100325<ref>PMID:25100325</ref>

-	~~Authors: Xu~~, N., Tamari, Y., Tochio, N., ~~Tate, S.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Solution structure of the peptidyl prolyl~~ cis-trans isomerase ~~domain of human Pin1 with sulfate ion~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Peptidylprolyl isomerase]]
		+	[[Category: Tamari, Y]]
		+	[[Category: Tate, S]]
		+	[[Category: Tochio, N]]
		+	[[Category: Xu, N]]
		+	[[Category: Isomerase]]
		+	[[Category: Ppiase]]
		+	[[Category: Protein/cis-trans-isomerase]]

OCA at 06:59, 23 April 2014

OCA — Wed, 23 Apr 2014 06:59:04 GMT

←Older revision		Revision as of 06:59, 23 April 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2ruc is ON HOLD	+	The entry 2ruc is ON HOLD until Paper Publication

	Authors: Xu, N., Tamari, Y., Tochio, N., Tate, S.		Authors: Xu, N., Tamari, Y., Tochio, N., Tate, S.

	Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion		Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion

OCA at 08:39, 16 April 2014

OCA — Wed, 16 Apr 2014 08:39:35 GMT

←Older revision		Revision as of 08:39, 16 April 2014
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	The entry 2ruc is ON HOLD		The entry 2ruc is ON HOLD

-	Authors: xu, n., ~~tamari~~, y., ~~tochio~~, n., ~~tate~~, s.	+	Authors: Xu, N., Tamari, Y., Tochio, N., Tate, S.

	Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion		Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion

OCA: Protected "2ruc" [edit=sysop:move=sysop]

OCA — Wed, 02 Apr 2014 08:06:08 GMT

Protected "2ruc" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:06, 2 April 2014

OCA: New page: '''Unreleased structure''' The entry 2ruc is ON HOLD Authors: xu, n., tamari, y., tochio, n., tate, s. Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain...

OCA — Wed, 02 Apr 2014 08:06:07 GMT

New page: '''Unreleased structure''' The entry 2ruc is ON HOLD Authors: xu, n., tamari, y., tochio, n., tate, s. Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain...

New page

'''Unreleased structure'''

The entry 2ruc is ON HOLD

Authors: xu, n., tamari, y., tochio, n., tate, s.

Description: Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion