3ey6 - Revision history

OCA at 06:37, 6 September 2023

OCA — Wed, 06 Sep 2023 06:37:13 GMT

←Older revision		Revision as of 06:37, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3ey6' size='340' side='right'caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>		<StructureSection load='3ey6' size='340' side='right'caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ey6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EY6 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;'>[[2f2d\|2f2d]], [[2awg\|2awg]]</div></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]] 1.05Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">FKBP38, FKBP8 ([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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [https://pdbe.org/3ey6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [https://pdbe.org/3ey6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN]] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>	+	[https://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Edlich F]]
-	[[Category: Edlich, F]]	+	[[Category: Fischer G]]
-	[[Category: Fischer, G]]	+	[[Category: Luecke C]]
-	[[Category: Luecke, C]]	+	[[Category: Maestre-Martinez M]]
-	[[Category: Maestre-Martinez, M]]	+	[[Category: Neumann P]]
-	[[Category: Neumann, P]]	+	[[Category: Parthier C]]
-	[[Category: Parthier, C]]	+	[[Category: Stubbs MT]]
-	[[Category: Stubbs~~, M T]]~~	+
-	~~[[Category: Apoptosis]]~~	+
-	~~[[Category: Beta half-barrel]]~~	+
-	~~[[Category: Host-virus interaction]]~~	+
-	~~[[Category: Immunophilin]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Mitochondrion]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Ppiase]]~~	+
-	~~[[Category: Rotamase]]~~	+
-	~~[[Category: Tpr repeat]]~~	+
-	~~[[Category: Transmembrane~~]]	+

OCA at 09:19, 23 February 2022

OCA — Wed, 23 Feb 2022 09:19:18 GMT

←Older revision		Revision as of 09:19, 23 February 2022
Line 1:		Line 1:

	==Crystal structure of the FK506-binding domain of human FKBP38==		==Crystal structure of the FK506-binding domain of human FKBP38==
-	<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>	+	<StructureSection load='3ey6' size='340' side='right'caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ey6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f2d\|2f2d]], [[2awg\|2awg]]</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;'>[[2f2d\|2f2d]], [[2awg\|2awg]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP38, FKBP8 ([~~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">FKBP38, FKBP8 ([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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [~~http~~://pdbe.org/3ey6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [https://pdbe.org/3ey6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN]] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>	+	[[https://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN]] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>
	== 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/ey/3ey6_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/3ey6_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 32:		Line 32:

	==See Also==		==See Also==
-	*[[~~FK506 binding protein~~\|~~FK506 binding protein~~]]	+	*[[FKBP 3D structures\|FKBP 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Edlich, F]]		[[Category: Edlich, F]]

OCA at 09:23, 25 October 2017

OCA — Wed, 25 Oct 2017 09:23:31 GMT

←Older revision		Revision as of 09:23, 25 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of the FK506-binding domain of human FKBP38==		==Crystal structure of the FK506-binding domain of human FKBP38==
	<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>		<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP38, FKBP8 ([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">FKBP38, FKBP8 ([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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://pdbe.org/3ey6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://pdbe.org/3ey6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ey6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 04:19, 10 February 2016

OCA — Wed, 10 Feb 2016 04:19:17 GMT

←Older revision		Revision as of 04:19, 10 February 2016
Line 2:		Line 2:
	<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>		<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f2d\|2f2d]], [[2awg\|2awg]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f2d\|2f2d]], [[2awg\|2awg]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP38, FKBP8 ([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">FKBP38, FKBP8 ([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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://pdbe.org/3ey6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<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=3ey6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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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 3ey6" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Edlich, F]]		[[Category: Edlich, F]]

OCA at 11:44, 25 December 2014

OCA — Thu, 25 Dec 2014 11:44:52 GMT

←Older revision		Revision as of 11:44, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f2d\|2f2d]], [[2awg\|2awg]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f2d\|2f2d]], [[2awg\|2awg]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP38, FKBP8 ([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">FKBP38, FKBP8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 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=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FKBP8_HUMAN FKBP8_HUMAN]] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: Edlich, F.]]	+	[[Category: Edlich, F]]
-	[[Category: Fischer, G.]]	+	[[Category: Fischer, G]]
-	[[Category: Luecke, C.]]	+	[[Category: Luecke, C]]
-	[[Category: Maestre-Martinez, M.]]	+	[[Category: Maestre-Martinez, M]]
-	[[Category: Neumann, P.]]	+	[[Category: Neumann, P]]
-	[[Category: Parthier, C.]]	+	[[Category: Parthier, C]]
-	[[Category: Stubbs, M T.]]	+	[[Category: Stubbs, M T]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
	[[Category: Beta half-barrel]]		[[Category: Beta half-barrel]]

OCA at 12:51, 29 September 2014

OCA — Mon, 29 Sep 2014 12:51:50 GMT

←Older revision		Revision as of 12:51, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~3ey6.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the FK506-binding domain of human FKBP38==
		+	<StructureSection load='3ey6' size='340' side='right' caption='[[3ey6]], [[Resolution\|resolution]] 1.05Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ey6]] 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=3EY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EY6 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f2d\|2f2d]], [[2awg\|2awg]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FKBP38, FKBP8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ey6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ey6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ey6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ey6 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/ey/3ey6_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 Bcl-2 inhibitor FKBP38 is regulated by the Ca(2+)-sensor calmodulin (CaM). Here we show a hitherto unknown low-affinity cation-binding site in the FKBP domain of FKBP38, which may afford an additional level of regulation based on electrostatic interactions. Fluorescence titration experiments indicate that in particular the physiologically relevant Ca(2+) ion binds to this site. NMR-based chemical shift perturbation data locate this cation-interaction site within the beta5-alpha1 loop (Leu90-Ile96) of the FKBP domain, which contains the acidic Asp92 and Asp94 side-chains. Binding constants were subsequently determined for K(+), Mg(2+), Ca(2+), and La(3+), indicating that the net charge and the radius of the ion influences the binding interaction. X-ray diffraction data furthermore show that the conformation of the beta5-alpha1 loop is influenced by the presence of a positively charged guanidinium group belonging to a neighboring FKBP38 molecule in the crystal lattice. The position of the cation-binding site has been further elucidated based on pseudocontact shift data obtained by NMR via titration with Tb(3+). Elimination of the Ca(2+)-binding capacity by substitution of the respective aspartate residues in a D92N/D94N double-substituted variant reduces the Bcl-2 affinity of the FKBP38(35-153)/CaM complex to the same degree as the presence of Ca(2+) in the wild-type protein. Hence, this charge-sensitive site in the FKBP domain participates in the regulation of FKBP38 function by enabling electrostatic interactions with ligand proteins and/or salt ions such as Ca(2+). Copyright (c) 2010 John Wiley & Sons, Ltd.

-	~~{{STRUCTURE_3ey6\| PDB=3ey6 \| SCENE= }}~~	+	A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding.,Maestre-Martinez M, Haupt K, Edlich F, Neumann P, Parthier C, Stubbs MT, Fischer G, Lucke C J Mol Recognit. 2011 Jan;24(1):23-34. PMID:20140889<ref>PMID:20140889</ref>

-	~~===Crystal structure~~ of the ~~FK506-binding domain of human FKBP38===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20140889}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3ey6]] 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=3EY6 OCA].~~	+

	==See Also==		==See Also==
	*[[FK506 binding protein\|FK506 binding protein]]		*[[FK506 binding protein\|FK506 binding protein]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020140889<~~/~~ref~~><~~ref group="xtra">PMID:016604427</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]

OCA at 16:18, 20 October 2012

OCA — Sat, 20 Oct 2012 16:18:22 GMT

←Older revision		Revision as of 16:18, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3ey6]] is a 1 chain structure ~~of [[FK506 binding protein]]~~ 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=3EY6 OCA].	+	[[3ey6]] 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=3EY6 OCA].

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

OCA at 21:14, 26 July 2012

OCA — Thu, 26 Jul 2012 21:14:31 GMT

←Older revision		Revision as of 21:14, 26 July 2012
Line 1:		Line 1:
	[[Image:3ey6.png\|left\|200px]]		[[Image:3ey6.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ey6", 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_3ey6\| PDB=3ey6 \| SCENE= }}		{{STRUCTURE_3ey6\| PDB=3ey6 \| SCENE= }}

	===Crystal structure of the FK506-binding domain of human FKBP38===		===Crystal structure of the FK506-binding domain of human FKBP38===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20140889}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20140889 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20140889}}		{{ABSTRACT_PUBMED_20140889}}

	==About this Structure==		==About this Structure==
-	[[3ey6]] 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=3EY6 OCA].	+	[[3ey6]] is a 1 chain structure of [[FK506 binding protein]] 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=3EY6 OCA].
		+
		+	==See Also==
		+	*[[FK506 binding protein\|FK506 binding protein]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20140889~~</ref><ref group="xtra">PMID:~~16604427~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020140889</ref><ref group="xtra">PMID:016604427</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
Line 32:		Line 24:
	[[Category: Parthier, C.]]		[[Category: Parthier, C.]]
	[[Category: Stubbs, M T.]]		[[Category: Stubbs, M T.]]
		+	[[Category: Apoptosis]]
		+	[[Category: Beta half-barrel]]
		+	[[Category: Host-virus interaction]]
		+	[[Category: Immunophilin]]
		+	[[Category: Isomerase]]
		+	[[Category: Membrane]]
		+	[[Category: Mitochondrion]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Ppiase]]
		+	[[Category: Rotamase]]
		+	[[Category: Tpr repeat]]
		+	[[Category: Transmembrane]]

OCA: Protected "3ey6" [edit=sysop:move=sysop]

OCA — Wed, 12 Jan 2011 05:22:53 GMT

Protected "3ey6" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:22, 12 January 2011

OCA at 05:22, 12 January 2011

OCA — Wed, 12 Jan 2011 05:22:51 GMT

←Older revision		Revision as of 05:22, 12 January 2011
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3ey6.png\|left\|200px]]
-	[[Image:3ey6.~~jpg~~\|left\|200px]]	+

	<!--		<!--
Line 12:		Line 11:
	===Crystal structure of the FK506-binding domain of human FKBP38===		===Crystal structure of the FK506-binding domain of human FKBP38===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20140889}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20140889 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20140889}}

	==About this Structure==		==About this Structure==
-	~~3EY6~~ is a 1 chain 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=3EY6 OCA].	+	[[3ey6]] 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=3EY6 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:16604427</ref><references group="xtra"/>	+	<ref group="xtra">PMID:20140889</ref><ref group="xtra">PMID:16604427</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
Line 27:		Line 32:
	[[Category: Parthier, C.]]		[[Category: Parthier, C.]]
	[[Category: Stubbs, M T.]]		[[Category: Stubbs, M T.]]
-	[[Category: Alternative splicing]]
-	[[Category: Apoptosis]]
-	[[Category: Beta half-barrel]]
-	[[Category: Calcium]]
-	[[Category: Host-virus interaction]]
-	[[Category: Immunophilin]]
-	[[Category: Isomerase]]
-	[[Category: Membrane]]
-	[[Category: Mitochondrion]]
-	[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
-	[[Category: Ppiase]]
-	[[Category: Rotamase]]
-	[[Category: Tpr repeat]]
-	[[Category: Transmembrane]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 28 13:49:20 2009''