4fru - Revision history

OCA at 15:32, 14 March 2024

2024-03-14T15:32:59Z

← Older revision		Revision as of 15:32, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fru]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRU FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fru]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRU FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.1Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [https://pdbe.org/4fru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [https://www.ebi.ac.uk/pdbsum/4fru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fru 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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [https://pdbe.org/4fru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [https://www.ebi.ac.uk/pdbsum/4fru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fru ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]		[https://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	ABSTRACT: BACKGROUND: Hyperelastosis cutis is an inherited autosomal recessive connective tissue disorder. Affected horses are characterized by hyperextensible skin, scarring, and severe lesions along the back. The disorder is caused by a mutation in cyclophilin B. RESULTS: The crystal structures of both wild-type and mutated (Gly6->Arg) horse cyclophilin B are presented. The mutation neither affects the overall fold of the enzyme nor impairs the catalytic site structure. Instead, it locally rearranges the flexible N-terminal end of the polypeptide chain and also makes it more rigid. CONCLUSIONS: Interactions of the mutated cyclophilin B with a set of endoplasmic reticulum-resident proteins must be affected.

	Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse.,Boudko SP, Ishikawa Y, Lerch TF, Nix J, Chapman MS, Bachinger HP BMC Res Notes. 2012 Nov 8;5:626. doi: 10.1186/1756-0500-5-626. PMID:23137129<ref>PMID:23137129</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4fru" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]		*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:07, 19 October 2022

2022-10-19T20:07:44Z

← Older revision		Revision as of 20:07, 19 October 2022
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	==Crystal structure of horse wild-type cyclophilin B==		==Crystal structure of horse wild-type cyclophilin B==
	<StructureSection load='4fru' size='340' side='right' caption='[[4fru]], [[Resolution\|resolution]] 1.10Å' scene=''>		<StructureSection load='4fru' size='340' side='right'caption='[[4fru]], [[Resolution\|resolution]] 1.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fru]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FRU FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fru]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRU FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [https://pdbe.org/4fru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [https://www.ebi.ac.uk/pdbsum/4fru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fru ProSAT]</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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [~~http~~://pdbe.org/4fru PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fru PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fru ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE]] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]		[https://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4fru" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fru" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
	[[Category: ~~Peptidylprolyl isomerase~~]]		[[Category: Large Structures]]
	[[Category: Bachinger~~, H P~~]]		[[Category: Bachinger HP]]
	[[Category: Boudko~~, S P~~]]		[[Category: Boudko SP]]
	[[Category: Ishikawa, Y]]		[[Category: Ishikawa Y]]
	~~[[Category: Chaperone]]~~
	~~[[Category: Cyclophilin-type ppiase]]~~
	~~[[Category: Endoplasmic reticulum]]~~
	~~[[Category: Foldase]]~~
	~~[[Category: Isomerase]]~~
	~~[[Category: Lh1 binding]]~~
	~~[[Category: P3h1-crtap-cypb complex]]~~
	~~[[Category: Peptidyl-prolyl cis-trans isomerase~~]]

OCA at 08:20, 15 November 2017

2017-11-15T08:20:07Z

← Older revision		Revision as of 08:20, 15 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4fru" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fru" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Cyclophilin\|Cyclophilin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:48, 5 August 2016

2016-08-05T06:48:34Z

← Older revision		Revision as of 06:48, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of horse wild-type cyclophilin B==		==Crystal structure of horse wild-type cyclophilin B==
	<StructureSection load='4fru' size='340' side='right' caption='[[4fru]], [[Resolution\|resolution]] 1.10Å' scene=''>		<StructureSection load='4fru' size='340' side='right' caption='[[4fru]], [[Resolution\|resolution]] 1.10Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [http://www.ebi.ac.uk/pdbsum/4fru 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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [http://pdbe.org/4fru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [http://www.ebi.ac.uk/pdbsum/4fru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fru ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 4fru" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Cyclophilin\|Cyclophilin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:38, 25 December 2014

2014-12-25T16:38:22Z

← Older revision		Revision as of 16:38, 25 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4fru~~\| ~~PDB~~=4fru \| ~~SCENE~~= }}		==Crystal structure of horse wild-type cyclophilin B==
	===~~Crystal structure~~ of ~~horse~~ wild-type cyclophilin B~~===~~		<StructureSection load='4fru' size='340' side='right' caption='[[4fru]], [[Resolution\|resolution]] 1.10Å' scene=''>
	~~{{ABSTRACT_PUBMED_23137129}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4fru]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FRU FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ME2:1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE'>ME2</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=4fru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fru OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fru RCSB], [http://www.ebi.ac.uk/pdbsum/4fru PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/A5YBL8_HORSE A5YBL8_HORSE]] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			ABSTRACT: BACKGROUND: Hyperelastosis cutis is an inherited autosomal recessive connective tissue disorder. Affected horses are characterized by hyperextensible skin, scarring, and severe lesions along the back. The disorder is caused by a mutation in cyclophilin B. RESULTS: The crystal structures of both wild-type and mutated (Gly6->Arg) horse cyclophilin B are presented. The mutation neither affects the overall fold of the enzyme nor impairs the catalytic site structure. Instead, it locally rearranges the flexible N-terminal end of the polypeptide chain and also makes it more rigid. CONCLUSIONS: Interactions of the mutated cyclophilin B with a set of endoplasmic reticulum-resident proteins must be affected.

	~~==About this Structure==~~		Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse.,Boudko SP, Ishikawa Y, Lerch TF, Nix J, Chapman MS, Bachinger HP BMC Res Notes. 2012 Nov 8;5:626. doi: 10.1186/1756-0500-5-626. PMID:23137129<ref>PMID:23137129</ref>
	~~[[4fru]] is a 1 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org~~/~~wiki/Equus_caballus Equus caballus]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin~~/~~ocashort?id=4FRU OCA].~~
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Bachinger, H P.]]		[[Category: Bachinger, H P]]
	[[Category: Boudko, S P.]]		[[Category: Boudko, S P]]
	[[Category: Ishikawa, Y.]]		[[Category: Ishikawa, Y]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Cyclophilin-type ppiase]]		[[Category: Cyclophilin-type ppiase]]

OCA at 09:19, 13 March 2013

2013-03-13T09:19:22Z

← Older revision		Revision as of 09:19, 13 March 2013
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	~~[[Image:4fru.png\|left\|200px]]~~

	{{STRUCTURE_4fru\| PDB=4fru \| SCENE= }}		{{STRUCTURE_4fru\| PDB=4fru \| SCENE= }}

	===Crystal structure of horse wild-type cyclophilin B===		===Crystal structure of horse wild-type cyclophilin B===

	{{ABSTRACT_PUBMED_23137129}}		{{ABSTRACT_PUBMED_23137129}}

OCA at 08:15, 9 January 2013

2013-01-09T08:15:18Z

← Older revision		Revision as of 08:15, 9 January 2013
Line 1:		Line 1:
	[[Image:4fru.~~jpg~~\|left\|200px]]		[[Image:4fru.png\|left\|200px]]

	{{STRUCTURE_4fru\| PDB=4fru \| SCENE= }}		{{STRUCTURE_4fru\| PDB=4fru \| SCENE= }}
Line 5:		Line 5:
	===Crystal structure of horse wild-type cyclophilin B===		===Crystal structure of horse wild-type cyclophilin B===

			{{ABSTRACT_PUBMED_23137129}}

	==About this Structure==		==About this Structure==

OCA at 06:58, 14 November 2012

2012-11-14T06:58:25Z

← Older revision		Revision as of 06:58, 14 November 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4fru.jpg\|left\|200px]]

	~~The entry~~ 4fru ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4fru\| PDB=4fru \| SCENE= }}

	~~Authors: Boudko, S.P., Ishikawa, Y., Bachinger, H.P.~~		===Crystal structure of horse wild-type cyclophilin B===

	~~Description~~: ~~Crystal structure of horse wild~~-type ~~cyclophilin B~~
			==About this Structure==
			[[4fru]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRU OCA].
			[[Category: Equus caballus]]
			[[Category: Peptidylprolyl isomerase]]
			[[Category: Bachinger, H P.]]
			[[Category: Boudko, S P.]]
			[[Category: Ishikawa, Y.]]
			[[Category: Chaperone]]
			[[Category: Cyclophilin-type ppiase]]
			[[Category: Endoplasmic reticulum]]
			[[Category: Foldase]]
			[[Category: Isomerase]]
			[[Category: Lh1 binding]]
			[[Category: P3h1-crtap-cypb complex]]
			[[Category: Peptidyl-prolyl cis-trans isomerase]]

OCA at 06:46, 25 July 2012

2012-07-25T06:46:55Z

← Older revision		Revision as of 06:46, 25 July 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4fru is ON HOLD		The entry 4fru is ON HOLD until Paper Publication

	Authors: Boudko, S.P., Ishikawa, Y., Bachinger, H.P.		Authors: Boudko, S.P., Ishikawa, Y., Bachinger, H.P.

	Description: Crystal structure of horse wild-type cyclophilin B		Description: Crystal structure of horse wild-type cyclophilin B

OCA at 05:02, 18 July 2012

2012-07-18T05:02:49Z

← Older revision		Revision as of 05:02, 18 July 2012
Line 3:		Line 3:
	The entry 4fru is ON HOLD		The entry 4fru is ON HOLD

	Authors: ~~BOUDKO~~, S.P., Ishikawa, Y., Bachinger, H.P.		Authors: Boudko, S.P., Ishikawa, Y., Bachinger, H.P.

	Description: Crystal structure of horse wild-type cyclophilin B		Description: Crystal structure of horse wild-type cyclophilin B