4r0x - Revision history

OCA at 17:42, 20 September 2023

OCA — Wed, 20 Sep 2023 17:42:01 GMT

←Older revision		Revision as of 17:42, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4r0x]] 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=4R0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R0X FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r0x]] 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=4R0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R0X FirstGlance]. <br>
-	</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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [https://pdbe.org/4r0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [https://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x ProSAT]</span></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]] 1.2Å</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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [https://pdbe.org/4r0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [https://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 14:03, 22 February 2023

OCA — Wed, 22 Feb 2023 14:03:50 GMT

←Older revision		Revision as of 14:03, 22 February 2023
Line 3:		Line 3:
	<StructureSection load='4r0x' size='340' side='right'caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>		<StructureSection load='4r0x' size='340' side='right'caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r0x]] 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=4R0X OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R0X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r0x]] 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=4R0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R0X FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AIG6, FKBP5, FKBP51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [https://pdbe.org/4r0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [https://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x 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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [~~http~~://pdbe.org/4r0x PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN]] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.	+	[https://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:

	==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: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Brecher M]]
-	[[Category: Brecher, M]]	+	[[Category: Hernandez G]]
-	[[Category: Hernandez, G]]	+	[[Category: Heroux A]]
-	[[Category: Heroux, A]]	+	[[Category: LeMaster DM]]
-	[[Category: LeMaster~~, D M~~]]	+	[[Category: Li HM]]
-	[[Category: Li~~, H M~~]]	+	[[Category: Mustafi SM]]
-	[[Category: Mustafi~~, S M~~]]	+	[[Category: Zhang J]]
-	[[Category: Zhang, J]]	+
-	~~[[Category: Fk-506 binding domain]]~~	+
-	~~[[Category: Hsp90 cochaperone]]~~	+
-	~~[[Category: Immunophiline]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Peptidyl-prolyl isomerase~~]]	+

OCA at 09:33, 24 April 2019

OCA — Wed, 24 Apr 2019 09:33:06 GMT

←Older revision		Revision as of 09:33, 24 April 2019
Line 1:		Line 1:

	==Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction==		==Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction==
-	<StructureSection load='4r0x' size='340' side='right' caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>	+	<StructureSection load='4r0x' size='340' side='right'caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r0x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r0x]] 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=4R0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0X FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AIG6, FKBP5, FKBP51 ([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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [http://pdbe.org/4r0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [http://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [http://pdbe.org/4r0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [http://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4r0x" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4r0x" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[FK506 binding protein\|FK506 binding protein]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Brecher, M]]		[[Category: Brecher, M]]

OCA at 14:18, 27 April 2017

OCA — Thu, 27 Apr 2017 14:18:38 GMT

←Older revision		Revision as of 14:18, 27 April 2017
Line 1:		Line 1:
		+
	==Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction==		==Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction==
	<StructureSection load='4r0x' size='340' side='right' caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>		<StructureSection load='4r0x' size='340' side='right' caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4r0x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0X FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r0x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0X FirstGlance]. <br>
	</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>		</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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [http://www.ebi.ac.uk/pdbsum/4r0x 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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [http://pdbe.org/4r0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [http://www.ebi.ac.uk/pdbsum/4r0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4r0x" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:28, 20 May 2015

OCA — Wed, 20 May 2015 06:28:21 GMT

←Older revision		Revision as of 06:28, 20 May 2015
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN]] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.		[[http://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN]] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Interchanging Leu 119 for Pro 119 at the tip of the beta4-beta5 loop in the first FK506 binding domain (FK1) of the FKBP51 and FKBP52 proteins, respectively, has been reported to largely reverse the inhibitory (FKBP51) or stimulatory (FKBP52) effects of these cochaperones on the transcriptional activity of glucocorticoid and androgen receptor protein complexes. Previous NMR relaxation studies have identified exchange linebroadening, indicative of submillisecond conformational motion, throughout the beta4-beta5 loop in the FK1 domain of FKBP51 which are suppressed by the FKBP52-like L119P substitution. This substitution also attenuates exchange linebroadening in the underlying beta2 and beta3a strands that is centered near a bifurcated mainchain hydrogen bond interaction between these two strands. The present study demonstrates that these exchange linebroadening effects arise from two distinct coupled conformational transitions, and the transition within the beta2 and beta3a strands samples a transient conformation which resembles the crystal structures of the selectively-inhibited FK1 domain of FKBP51 recently reported by Hausch and colleagues. Although the crystal structures for their series of inhibitors were interpreted as evidence for an induced fit mechanism of association, the presence of a similar conformation being significantly populated in the unliganded FKBP51 domain is more consistent with a conformational selection binding process. The contrastingly reduced conformational plasticity of the corresponding FK1 domain of FKBP52 is consistent with the current model in which FKBP51 binds to both the apo- and hormone-bound forms of the steroid receptor to modulate its affinity for ligand, while FKBP52 binds selectively to the latter state.
		+
		+	Coupling of conformational transitions in the N-terminal domain of the 51 kDa FK506-binding protein (FKBP51) near its site of interaction with the steroid receptor proteins.,LeMaster DM, Mustafi SM, Brecher M, Zhang J, Heroux A, Li H, Hernandez G J Biol Chem. 2015 May 7. pii: jbc.M115.650655. PMID:25953903<ref>PMID:25953903</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:22, 13 May 2015

OCA — Wed, 13 May 2015 12:22:50 GMT

←Older revision		Revision as of 12:22, 13 May 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction==
-		+	<StructureSection load='4r0x' size='340' side='right' caption='[[4r0x]], [[Resolution\|resolution]] 1.20Å' scene=''>
-	~~The entry~~ 4r0x is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4r0x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0X FirstGlance]. <br>
-	~~Authors~~: ~~LeMaster, D~~.M., ~~Mustafi, S~~.M.~~, Brecher, M~~.~~, Zhang, J~~.~~, Heroux, A~~., ~~Li, H~~.M., ~~Hernandez~~, G.	+	</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=4r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r0x RCSB], [http://www.ebi.ac.uk/pdbsum/4r0x PDBsum]</span></td></tr>
-	~~Description: Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction~~	+	</table>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	== Function ==
-	[[Category: ~~Li, H.M~~]]	+	[[http://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN]] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Peptidylprolyl isomerase]]
	[[Category: Brecher, M]]		[[Category: Brecher, M]]
-	[[Category: Lemaster, D.M]]
-	[[Category: Mustafi, S.M]]
	[[Category: Hernandez, G]]		[[Category: Hernandez, G]]
	[[Category: Heroux, A]]		[[Category: Heroux, A]]
		+	[[Category: LeMaster, D M]]
		+	[[Category: Li, H M]]
		+	[[Category: Mustafi, S M]]
	[[Category: Zhang, J]]		[[Category: Zhang, J]]
		+	[[Category: Fk-506 binding domain]]
		+	[[Category: Hsp90 cochaperone]]
		+	[[Category: Immunophiline]]
		+	[[Category: Isomerase]]
		+	[[Category: Peptidyl-prolyl isomerase]]

OCA at 16:21, 24 December 2014

OCA — Wed, 24 Dec 2014 16:21:36 GMT

←Older revision		Revision as of 16:21, 24 December 2014
Line 6:		Line 6:

	Description: Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction		Description: Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction
		+	[[Category: Unreleased Structures]]
		+	[[Category: Li, H.M]]
		+	[[Category: Brecher, M]]
		+	[[Category: Lemaster, D.M]]
		+	[[Category: Mustafi, S.M]]
		+	[[Category: Hernandez, G]]
		+	[[Category: Heroux, A]]
		+	[[Category: Zhang, J]]

OCA at 08:19, 24 September 2014

OCA — Wed, 24 Sep 2014 08:19:40 GMT

←Older revision		Revision as of 08:19, 24 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4r0x is ON HOLD	+	The entry 4r0x is ON HOLD until Paper Publication

	Authors: LeMaster, D.M., Mustafi, S.M., Brecher, M., Zhang, J., Heroux, A., Li, H.M., Hernandez, G.		Authors: LeMaster, D.M., Mustafi, S.M., Brecher, M., Zhang, J., Heroux, A., Li, H.M., Hernandez, G.

	Description: Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction		Description: Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction

OCA: Protected "4r0x" [edit=sysop:move=sysop]

OCA — Wed, 13 Aug 2014 07:47:28 GMT

Protected "4r0x" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:47, 13 August 2014

OCA: New page: '''Unreleased structure''' The entry 4r0x is ON HOLD Authors: LeMaster, D.M., Mustafi, S.M., Brecher, M., Zhang, J., Heroux, A., Li, H.M., Hernandez, G. Description: Allosteric couplin...

OCA — Wed, 13 Aug 2014 07:47:27 GMT

New page: '''Unreleased structure''' The entry 4r0x is ON HOLD Authors: LeMaster, D.M., Mustafi, S.M., Brecher, M., Zhang, J., Heroux, A., Li, H.M., Hernandez, G. Description: Allosteric couplin...

New page

'''Unreleased structure'''

The entry 4r0x is ON HOLD

Authors: LeMaster, D.M., Mustafi, S.M., Brecher, M., Zhang, J., Heroux, A., Li, H.M., Hernandez, G.

Description: Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction