5cyh - Revision history

OCA at 12:22, 6 March 2024

OCA — Wed, 06 Mar 2024 12:22:29 GMT

←Older revision		Revision as of 12:22, 6 March 2024
Line 1:		Line 1:

	==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO==		==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO==
-	<StructureSection load='5cyh' size='340' side='right' caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='5cyh' size='340' side='right'caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cyh]] 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=5CYH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CYH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cyh]] 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=5CYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CYH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=GLY:GLYCINE'>GLY</scene~~>, ~~<scene name='pdbligand=PRO:PROLINE'>PRO</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]] 2.1Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CYCLOPHILIN ([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=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [~~http~~://pdbe.org/5cyh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5cyh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5cyh 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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [https://pdbe.org/5cyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [https://www.ebi.ac.uk/pdbsum/5cyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cyh ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/5cyh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/5cyh_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 18:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5cyh ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5cyh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The structures of cyclophilin A complexed with dipeptides of Ser-Pro, His-Pro, and Gly-Pro have been determined and refined at high resolution. Comparison of these structures revealed that the dipeptide complexes have the same molecular conformation and the same binding of the dipeptides. The side chains of the N-terminal amino acid of the above dipeptides do not strongly interact with cyclophilin, implying their minor contribution to the cis-trans isomerization and thus accounting for the broad catalytic specificity of the enzyme. The binding of the dipeptides is similar to that of the common substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide in terms of the N-terminal hydrogen bonding and the hydrophobic interaction of the proline side chain. However, substantial difference between these structures are observed in (1) hydrogen bonding between the carboxyl terminus of the peptides and Arg55 and between Arg55 and Gln63, (2) the side chain conformation of Arg55, and (3) water binding at the active site. These differences imply either that dipeptides are not substrates but competitive inhibitors of peptidyl-prolyl cis-trans isomerases or that dipeptides are subject to different catalytic mechanisms from tetrapeptides.

-	~~Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes.,Zhao Y, Ke H Biochemistry. 1996 Jun 11;35(23):7362-8. PMID:8652512<ref>PMID:8652512</ref>~~	+	==See Also==
-		+	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 5cyh" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Ke, H~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Zhao, Y~~]]	+	[[Category: Ke H]]
-	[[Category: ~~Binding protein for cyclosporin some]]~~	+	[[Category: Zhao Y]]
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Cyclophilin]]~~	+
-	~~[[Category: Isomerase~~]]	+

OCA at 07:23, 29 November 2017

OCA — Wed, 29 Nov 2017 07:23:19 GMT

←Older revision		Revision as of 07:23, 29 November 2017
Line 1:		Line 1:
		+
	==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO==		==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO==
	<StructureSection load='5cyh' size='340' side='right' caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='5cyh' size='340' side='right' caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([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">CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [http://pdbe.org/5cyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [http://www.ebi.ac.uk/pdbsum/5cyh 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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [http://pdbe.org/5cyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [http://www.ebi.ac.uk/pdbsum/5cyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cyh ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 26:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 5cyh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5cyh" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cyclophilin\|Cyclophilin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:22, 9 February 2016

OCA — Tue, 09 Feb 2016 00:22:56 GMT

←Older revision		Revision as of 00:22, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='5cyh' size='340' side='right' caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='5cyh' size='340' side='right' caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cyh]] 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=5CYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CYH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cyh]] 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=5CYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CYH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([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">CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [http://www.ebi.ac.uk/pdbsum/5cyh 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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [http://pdbe.org/5cyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [http://www.ebi.ac.uk/pdbsum/5cyh PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 15:		Line 15:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5cyh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 25:		Line 25:
	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 5cyh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ke, H]]		[[Category: Ke, H]]
	[[Category: Zhao, Y]]		[[Category: Zhao, Y]]

OCA at 17:05, 10 December 2014

OCA — Wed, 10 Dec 2014 17:05:56 GMT

←Older revision		Revision as of 17:05, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~5cyh.~~png~~\|~~left~~\|200px]]	+	==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO==
		+	<StructureSection load='5cyh' size='340' side='right' caption='[[5cyh]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5cyh]] 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=5CYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CYH FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=5cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5cyh RCSB], [http://www.ebi.ac.uk/pdbsum/5cyh PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/5cyh_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The structures of cyclophilin A complexed with dipeptides of Ser-Pro, His-Pro, and Gly-Pro have been determined and refined at high resolution. Comparison of these structures revealed that the dipeptide complexes have the same molecular conformation and the same binding of the dipeptides. The side chains of the N-terminal amino acid of the above dipeptides do not strongly interact with cyclophilin, implying their minor contribution to the cis-trans isomerization and thus accounting for the broad catalytic specificity of the enzyme. The binding of the dipeptides is similar to that of the common substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide in terms of the N-terminal hydrogen bonding and the hydrophobic interaction of the proline side chain. However, substantial difference between these structures are observed in (1) hydrogen bonding between the carboxyl terminus of the peptides and Arg55 and between Arg55 and Gln63, (2) the side chain conformation of Arg55, and (3) water binding at the active site. These differences imply either that dipeptides are not substrates but competitive inhibitors of peptidyl-prolyl cis-trans isomerases or that dipeptides are subject to different catalytic mechanisms from tetrapeptides.

-	~~{{STRUCTURE_5cyh\| PDB=5cyh \| SCENE= }}~~	+	Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes.,Zhao Y, Ke H Biochemistry. 1996 Jun 11;35(23):7362-8. PMID:8652512<ref>PMID:8652512</ref>

-	~~===CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8652512}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[5cyh]] 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=5CYH OCA].~~	+

	==See Also==		==See Also==
	*[[Cyclophilin\|Cyclophilin]]		*[[Cyclophilin\|Cyclophilin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008652512<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Ke, H.]]	+	[[Category: Ke, H]]
-	[[Category: Zhao, Y.]]	+	[[Category: Zhao, Y]]
	[[Category: Binding protein for cyclosporin some]]		[[Category: Binding protein for cyclosporin some]]
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Cyclophilin]]		[[Category: Cyclophilin]]
	[[Category: Isomerase]]		[[Category: Isomerase]]

OCA at 11:59, 20 October 2012

OCA — Sat, 20 Oct 2012 11:59:10 GMT

←Older revision		Revision as of 11:59, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[5cyh]] is a 1 chain structure ~~of [[Cyclophilin]]~~ 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=5CYH OCA].	+	[[5cyh]] 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=5CYH OCA].

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

OCA at 07:14, 26 July 2012

OCA — Thu, 26 Jul 2012 07:14:55 GMT

←Older revision		Revision as of 07:14, 26 July 2012
Line 1:		Line 1:
	[[Image:5cyh.png\|left\|200px]]		[[Image:5cyh.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_5cyh", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_5cyh\| PDB=5cyh \| SCENE= }}		{{STRUCTURE_5cyh\| PDB=5cyh \| SCENE= }}

	===CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO===		===CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8652512}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8652512 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8652512}}		{{ABSTRACT_PUBMED_8652512}}

Line 22:		Line 11:

	==See Also==		==See Also==
-	*[[Cyclophilin]]	+	*[[Cyclophilin\|Cyclophilin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~8652512~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008652512</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ke, H.]]		[[Category: Ke, H.]]
Line 32:		Line 21:
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Cyclophilin]]		[[Category: Cyclophilin]]
		+	[[Category: Isomerase]]

OCA: Protected "5cyh" [edit=sysop:move=sysop]

OCA — Sun, 26 Dec 2010 09:34:48 GMT

Protected "5cyh" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:34, 26 December 2010

OCA at 09:34, 26 December 2010

OCA — Sun, 26 Dec 2010 09:34:47 GMT

←Older revision		Revision as of 09:34, 26 December 2010
Line 1:		Line 1:
-	{{Seed}}
	[[Image:5cyh.png\|left\|200px]]		[[Image:5cyh.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~5CYH~~ is a ~~2 chains~~ structure of ~~sequences~~ 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=5CYH OCA].	+	[[5cyh]] is a 1 chain structure of [[Cyclophilin]] 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=5CYH OCA].
		+
		+	==See Also==
		+	*[[Cyclophilin]]

	==Reference==		==Reference==
Line 30:		Line 32:
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Cyclophilin]]		[[Category: Cyclophilin]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:51:04 2009''

OCA at 02:51, 17 February 2009

OCA — Tue, 17 Feb 2009 02:51:09 GMT

←Older revision		Revision as of 02:51, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	5CYH is a ~~[[Single protein]]~~ structure of ~~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=5CYH OCA].	+	5CYH is a 2 chains structure of sequences 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=5CYH OCA].

	==Reference==		==Reference==
-	~~Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes., Zhao Y, Ke H, Biochemistry. 1996 Jun 11;35(23):7362-8.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/8652512 8652512]~~	+	<ref group="xtra">PMID:8652512</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Ke, H.]]		[[Category: Ke, H.]]
	[[Category: Zhao, Y.]]		[[Category: Zhao, Y.]]
Line 32:		Line 31:
	[[Category: Cyclophilin]]		[[Category: Cyclophilin]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Jul 3 14~~:00:~~03 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:51:04 2009''

OCA at 11:00, 3 July 2008

OCA — Thu, 03 Jul 2008 11:00:03 GMT

←Older revision		Revision as of 11:00, 3 July 2008
Line 1:		Line 1:
-	[[Image:5cyh.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:5cyh.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_5cyh\| PDB=5cyh \| SCENE= }}		{{STRUCTURE_5cyh\| PDB=5cyh \| SCENE= }}

-	~~'''~~CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO~~'''~~	+	===CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO===


-	~~==Overview==~~	+	<!--
-	The ~~structures of cyclophilin A complexed with dipeptides of Ser-Pro~~, ~~His-Pro~~, ~~and Gly-Pro have been determined and refined at high resolution. Comparison of these structures revealed that~~ the dipeptide complexes have the same molecular conformation and the same binding of the dipeptides. The side chains of the N-terminal amino acid of the above dipeptides do not strongly interact with cyclophilin, implying their minor contribution to the ~~cis-trans isomerization and thus accounting for the broad catalytic specificity of the enzyme~~. The binding of the dipeptides is similar to that of the common substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide in terms of the N-terminal hydrogen bonding and the hydrophobic interaction of the proline side chain. ~~However, substantial difference between these structures are observed in (1~~) ~~hydrogen bonding between the carboxyl terminus of the peptides and Arg55 and between Arg55 and Gln63~~, ~~(2)~~ the ~~side chain conformation of Arg55, and (3) water binding at the active site~~. ~~These differences imply either that dipeptides are not substrates but competitive inhibitors of peptidyl~~-~~prolyl cis~~-~~trans isomerases or that dipeptides are subject to different catalytic mechanisms from tetrapeptides.~~	+	The line below this paragraph, {{ABSTRACT_PUBMED_8652512}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 8652512 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_8652512}}

	==About this Structure==		==About this Structure==
Line 27:		Line 31:
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Cyclophilin]]		[[Category: Cyclophilin]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Apr 30 13~~:59:05 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:00:03 2008''