4lax - Revision history

OCA at 16:15, 20 September 2023

OCA — Wed, 20 Sep 2023 16:15:40 GMT

←Older revision		Revision as of 16:15, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4lax]] 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=4LAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4lax]] 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=4LAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.007Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [https://pdbe.org/4lax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [https://www.ebi.ac.uk/pdbsum/4lax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lax 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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [https://pdbe.org/4lax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [https://www.ebi.ac.uk/pdbsum/4lax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lax ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:48, 14 December 2022

OCA — Wed, 14 Dec 2022 10:48:55 GMT

←Older revision		Revision as of 10:48, 14 December 2022
Line 1:		Line 1:

	==Crystal Structure Analysis of FKBP52, Complex with FK506==		==Crystal Structure Analysis of FKBP52, Complex with FK506==
-	<StructureSection load='4lax' size='340' side='right' caption='[[4lax]], [[Resolution\|resolution]] 2.01Å' scene=''>	+	<StructureSection load='4lax' size='340' side='right'caption='[[4lax]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lax]] 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=4LAX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LAX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lax]] 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=4LAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1c\|1q1c]], [[4lav\|4lav]], [[4law\|4law]], [[4lay\|4lay]]</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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [https://pdbe.org/4lax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [https://www.ebi.ac.uk/pdbsum/4lax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lax ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP4, FKBP52 ([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='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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [~~http~~://pdbe.org/4lax PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4lax PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4lax ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN]] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>	+	[https://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[~~FK506 binding protein~~\|~~FK506 binding protein~~]]	+	*[[FKBP 3D structures\|FKBP 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Peptidylprolyl isomerase~~]]	+	[[Category: Large Structures]]
-	[[Category: Bracher, A]]	+	[[Category: Bracher A]]
-	[[Category: Haehle, A]]	+	[[Category: Haehle A]]
-	[[Category: Hausch, F]]	+	[[Category: Hausch F]]
-	[[Category: Kozany, C]]	+	[[Category: Kozany C]]
-	[[Category: Wild, P]]	+	[[Category: Wild P]]
-	[[Category: Zacharias, M]]	+	[[Category: Zacharias M]]
-	~~[[Category: Fk-506 binding domain]]~~	+
-	~~[[Category: Hsp90 cochaperone]]~~	+
-	~~[[Category: Immunophilin]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Peptidyl-prolyl isomerase]]~~	+
-	~~[[Category: Protein folding~~]]	+

OCA at 07:33, 4 August 2016

OCA — Thu, 04 Aug 2016 07:33:20 GMT

←Older revision		Revision as of 07:33, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure Analysis of FKBP52, Complex with FK506==		==Crystal Structure Analysis of FKBP52, Complex with FK506==
	<StructureSection load='4lax' size='340' side='right' caption='[[4lax]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='4lax' size='340' side='right' caption='[[4lax]], [[Resolution\|resolution]] 2.01Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP4, FKBP52 ([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">FKBP4, FKBP52 ([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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [http://www.ebi.ac.uk/pdbsum/4lax 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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [http://pdbe.org/4lax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [http://www.ebi.ac.uk/pdbsum/4lax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lax ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4lax" style="background-color:#fffaf0;"></div>

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

OCA at 06:57, 25 December 2014

OCA — Thu, 25 Dec 2014 06:57:37 GMT

←Older revision		Revision as of 06:57, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4lax\| PDB=4lax \| SCENE= }}~~	+	==Crystal Structure Analysis of FKBP52, Complex with FK506==
-	===Crystal Structure Analysis of FKBP52, Complex with FK506===	+	<StructureSection load='4lax' size='340' side='right' caption='[[4lax]], [[Resolution\|resolution]] 2.01Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23933011}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4lax]] 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=4LAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LAX FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q1c\|1q1c]], [[4lav\|4lav]], [[4law\|4law]], [[4lay\|4lay]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP4, FKBP52 ([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='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=4lax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lax OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lax RCSB], [http://www.ebi.ac.uk/pdbsum/4lax PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN]] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>		[[http://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN]] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The human Hsp90 co-chaperone FKBP52 belongs to the family of FK506-binding proteins, which act as peptidyl-prolyl isomerases. FKBP52 specifically enhances the signaling of steroid hormone receptors, modulates ion channels and regulates neuronal outgrowth dynamics. In turn, small-molecule ligands of FKBP52 have been suggested as potential neurotrophic or anti-prostate cancer agents. The usefulness of available ligands is however limited by a lack of selectivity. The immunophilin FKBP52 is composed of three domains, an FK506-binding domain with peptidyl-prolyl isomerase activity, an FKBP-like domain of unknown function and a TPR-clamp domain, which recognizes the C-terminal peptide of Hsp90 with high affinity. The herein reported crystal structures of FKBP52 reveal that the short linker connecting the FK506-binding domain and the FKBP-like domain acts as a flexible hinge. This enhanced flexibility and its modulation by phosphorylation might explain some of the functional antagonism between the closely related homologs FKBP51 and FKBP52. We further present two co-crystal structures of FKBP52 in complex with the prototypic ligand FK506 and a synthetic analog thereof. These structures revealed the molecular interactions in great detail, which enabled in-depth comparison with the corresponding complexes of the other cytosolic FKBPs, FKBP51 and FKBP12. The observed subtle differences provide crucial insights for the rational design of ligands with improved selectivity for FKBP52.
		+
		+	Crystal Structures of the Free and Ligand-Bound FK1-FK2 Domain Segment of FKBP52 Reveal a Flexible Inter-Domain Hinge.,Bracher A, Kozany C, Hahle A, Wild P, Zacharias M, Hausch F J Mol Biol. 2013 Aug 8. pii: S0022-2836(13)00502-0. doi:, 10.1016/j.jmb.2013.07.041. PMID:23933011<ref>PMID:23933011</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4lax]] 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=4LAX OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023933011</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[FK506 binding protein\|FK506 binding protein]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: Bracher, A.]]	+	[[Category: Bracher, A]]
-	[[Category: Haehle, A.]]	+	[[Category: Haehle, A]]
-	[[Category: Hausch, F.]]	+	[[Category: Hausch, F]]
-	[[Category: Kozany, C.]]	+	[[Category: Kozany, C]]
-	[[Category: Wild, P.]]	+	[[Category: Wild, P]]
-	[[Category: Zacharias, M.]]	+	[[Category: Zacharias, M]]
	[[Category: Fk-506 binding domain]]		[[Category: Fk-506 binding domain]]
	[[Category: Hsp90 cochaperone]]		[[Category: Hsp90 cochaperone]]

OCA at 06:17, 13 November 2013

OCA — Wed, 13 Nov 2013 06:17:17 GMT

←Older revision		Revision as of 06:17, 13 November 2013
Line 7:		Line 7:

	==About this Structure==		==About this Structure==
-	[[4lax]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ochroconis_lascauxensis Ochroconis lascauxensis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAX OCA].	+	[[4lax]] 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=4LAX OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:023933011</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:023933011</ref><references group="xtra"/><references/>
-	[[Category: ~~Ochroconis lascauxensis~~]]	+	[[Category: Human]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Bracher, A.]]		[[Category: Bracher, A.]]

OCA at 05:28, 28 August 2013

OCA — Wed, 28 Aug 2013 05:28:58 GMT

←Older revision		Revision as of 05:28, 28 August 2013
Line 1:		Line 1:
	{{STRUCTURE_4lax\| PDB=4lax \| SCENE= }}		{{STRUCTURE_4lax\| PDB=4lax \| SCENE= }}
	===Crystal Structure Analysis of FKBP52, Complex with FK506===		===Crystal Structure Analysis of FKBP52, Complex with FK506===
		+	{{ABSTRACT_PUBMED_23933011}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023933011</ref><references group="xtra"/><references/>
	[[Category: Ochroconis lascauxensis]]		[[Category: Ochroconis lascauxensis]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]

OCA at 08:36, 21 August 2013

OCA — Wed, 21 Aug 2013 08:36:47 GMT

←Older revision		Revision as of 08:36, 21 August 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4lax\| PDB=4lax \| SCENE= }}
		+	===Crystal Structure Analysis of FKBP52, Complex with FK506===

-	The ~~entry 4lax is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN]] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>

-	~~Authors~~: ~~Bracher, A~~.~~, Kozany, C~~.~~, Haehle, A~~.~~, Wild, P~~.~~, Zacharias, M~~.~~, Hausch, F~~.	+	==About this Structure==
		+	[[4lax]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochroconis_lascauxensis Ochroconis lascauxensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAX OCA].

-	~~Description~~: ~~Crystal Structure Analysis of FKBP52~~, ~~Complex with FK506~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Ochroconis lascauxensis]]
		+	[[Category: Peptidylprolyl isomerase]]
		+	[[Category: Bracher, A.]]
		+	[[Category: Haehle, A.]]
		+	[[Category: Hausch, F.]]
		+	[[Category: Kozany, C.]]
		+	[[Category: Wild, P.]]
		+	[[Category: Zacharias, M.]]
		+	[[Category: Fk-506 binding domain]]
		+	[[Category: Hsp90 cochaperone]]
		+	[[Category: Immunophilin]]
		+	[[Category: Isomerase]]
		+	[[Category: Peptidyl-prolyl isomerase]]
		+	[[Category: Protein folding]]

OCA at 07:15, 14 August 2013

OCA — Wed, 14 Aug 2013 07:15:28 GMT

←Older revision		Revision as of 07:15, 14 August 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4lax is ON HOLD	+	The entry 4lax is ON HOLD until Paper Publication

	Authors: Bracher, A., Kozany, C., Haehle, A., Wild, P., Zacharias, M., Hausch, F.		Authors: Bracher, A., Kozany, C., Haehle, A., Wild, P., Zacharias, M., Hausch, F.

	Description: Crystal Structure Analysis of FKBP52, Complex with FK506		Description: Crystal Structure Analysis of FKBP52, Complex with FK506

OCA at 04:45, 18 July 2013

OCA — Thu, 18 Jul 2013 04:45:52 GMT

←Older revision		Revision as of 04:45, 18 July 2013
Line 5:		Line 5:
	Authors: Bracher, A., Kozany, C., Haehle, A., Wild, P., Zacharias, M., Hausch, F.		Authors: Bracher, A., Kozany, C., Haehle, A., Wild, P., Zacharias, M., Hausch, F.

-	Description: Crystal Structure Analysis of FKBP52. Complex with FK506	+	Description: Crystal Structure Analysis of FKBP52, Complex with FK506

OCA: Protected "4lax" [edit=sysop:move=sysop]

OCA — Sun, 30 Jun 2013 09:11:57 GMT

Protected "4lax" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:11, 30 June 2013