6kke - Revision history

OCA at 10:35, 22 November 2023

OCA — Wed, 22 Nov 2023 10:35:22 GMT

←Older revision		Revision as of 10:35, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='6kke' size='340' side='right'caption='[[6kke]], [[Resolution\|resolution]] 2.58Å' scene=''>		<StructureSection load='6kke' size='340' side='right'caption='[[6kke]], [[Resolution\|resolution]] 2.58Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6kke]] is a 2 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=6KKE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6KKE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6kke]] is a 2 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=6KKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KKE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=8HO:2~~-[~~(1-methyl-4-oxidanyl-7-phenoxy-isoquinolin-3-yl)carbonylamino~~]~~ethanoic+acid'>8HO</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]] 2.577Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[6acm\|6acm]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8HO:2-[(1-methyl-4-oxidanyl-7-phenoxy-isoquinolin-3-yl)carbonylamino]ethanoic+acid'>8HO</scene></td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~"><b>[~~[Gene\|Gene:~~]~~]</b~~></td>~~<td class="sblockDat">THRB, ERBA2, NR1A2, THR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kke OCA], [https://pdbe.org/6kke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kke RCSB], [https://www.ebi.ac.uk/pdbsum/6kke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kke 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=6kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kke OCA], [~~http~~://pdbe.org/6kke PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6kke RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6kke PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6kke ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/THB_HUMAN THB_HUMAN]] Defects in THRB are the cause of generalized thyroid hormone resistance (GTHR) [MIM:[~~http~~://omim.org/entry/188570 188570]]. GTHR is a disease characterized by goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. GTHR patients also have high levels of circulating thyroid hormones (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH).<ref>PMID:2510172</ref> <ref>PMID:2153155</ref> <ref>PMID:1846005</ref> <ref>PMID:1661299</ref> <ref>PMID:1653889</ref> <ref>PMID:1563081</ref> <ref>PMID:1314846</ref> <ref>PMID:1619012</ref> <ref>PMID:1587388</ref> <ref>PMID:1324420</ref> <ref>PMID:8514853</ref> <ref>PMID:8175986</ref> <ref>PMID:7833659</ref> <ref>PMID:8664910</ref> <ref>PMID:8889584</ref> <ref>PMID:10660344</ref> <ref>PMID:16804041</ref> <ref>PMID:19268523</ref> Defects in THRB are the cause of generalized thyroid hormone resistance autosomal recessive (GTHRAR) [MIM:[~~http~~://omim.org/entry/274300 274300]]. An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone. Defects in THRB are the cause of selective pituitary thyroid hormone resistance (PRTH) [MIM:[~~http~~://omim.org/entry/145650 145650]]; also known as familial hyperthyroidism due to inappropriate thyrotropin secretion. PRTH is a variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established.<ref>PMID:7528740</ref> <ref>PMID:8381821</ref>	+	[https://www.uniprot.org/uniprot/THB_HUMAN THB_HUMAN] Defects in THRB are the cause of generalized thyroid hormone resistance (GTHR) [MIM:[https://omim.org/entry/188570 188570]. GTHR is a disease characterized by goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. GTHR patients also have high levels of circulating thyroid hormones (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH).<ref>PMID:2510172</ref> <ref>PMID:2153155</ref> <ref>PMID:1846005</ref> <ref>PMID:1661299</ref> <ref>PMID:1653889</ref> <ref>PMID:1563081</ref> <ref>PMID:1314846</ref> <ref>PMID:1619012</ref> <ref>PMID:1587388</ref> <ref>PMID:1324420</ref> <ref>PMID:8514853</ref> <ref>PMID:8175986</ref> <ref>PMID:7833659</ref> <ref>PMID:8664910</ref> <ref>PMID:8889584</ref> <ref>PMID:10660344</ref> <ref>PMID:16804041</ref> <ref>PMID:19268523</ref> Defects in THRB are the cause of generalized thyroid hormone resistance autosomal recessive (GTHRAR) [MIM:[https://omim.org/entry/274300 274300]. An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone. Defects in THRB are the cause of selective pituitary thyroid hormone resistance (PRTH) [MIM:[https://omim.org/entry/145650 145650]; also known as familial hyperthyroidism due to inappropriate thyrotropin secretion. PRTH is a variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established.<ref>PMID:7528740</ref> <ref>PMID:8381821</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/THB_HUMAN THB_HUMAN]] High affinity receptor for triiodothyronine.<ref>PMID:17418816</ref>	+	[https://www.uniprot.org/uniprot/THB_HUMAN THB_HUMAN] High affinity receptor for triiodothyronine.<ref>PMID:17418816</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Li, Y]]	+	[[Category: Li Y]]
-	[[Category: Yao~~, B Q]]~~	+	[[Category: Yao BQ]]
-	~~[[Category: Agonist]]~~	+
-	~~[[Category: Anemia]]~~	+
-	~~[[Category: Thyroid hormone receptor]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 07:09, 4 March 2020

OCA — Wed, 04 Mar 2020 07:09:27 GMT

←Older revision		Revision as of 07:09, 4 March 2020
Line 3:		Line 3:
	<StructureSection load='6kke' size='340' side='right'caption='[[6kke]], [[Resolution\|resolution]] 2.58Å' scene=''>		<StructureSection load='6kke' size='340' side='right'caption='[[6kke]], [[Resolution\|resolution]] 2.58Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6kke]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KKE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6kke]] is a 2 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=6KKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KKE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8HO:2-[(1-methyl-4-oxidanyl-7-phenoxy-isoquinolin-3-yl)carbonylamino]ethanoic+acid'>8HO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8HO:2-[(1-methyl-4-oxidanyl-7-phenoxy-isoquinolin-3-yl)carbonylamino]ethanoic+acid'>8HO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6acm\|6acm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6acm\|6acm]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">THRB, ERBA2, NR1A2, THR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kke OCA], [http://pdbe.org/6kke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kke RCSB], [http://www.ebi.ac.uk/pdbsum/6kke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kke 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=6kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kke OCA], [http://pdbe.org/6kke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kke RCSB], [http://www.ebi.ac.uk/pdbsum/6kke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kke ProSAT]</span></td></tr>
	</table>		</table>
Line 14:		Line 15:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~Nuclear receptors are important transcriptional factors that share high sequence identity and conserved domains, including a DNA-binding domain~~ (~~DBD~~) and a ligand-binding ~~domain~~ (~~LBD~~). ~~The LBD plays~~ a ~~crucial role~~ in ~~ligand-mediated nuclear receptor activity. Hundreds of different crystal structures of nuclear receptors have revealed~~ a ~~general mechanism for~~ the ~~molecular basis~~ of ~~ligand binding and ligand-mediated regulation of nuclear receptors~~. Despite the ~~conserved fold of nuclear~~ receptor ~~LBDs~~, ~~the ligand-binding pocket is the least conserved region among~~ different ~~nuclear receptor LBDs. Structural comparison and analysis show that several features of~~ the ~~pocket~~, ~~like~~ the ~~size and also the shape, have contributed to the ligand~~ binding ~~affinity and specificity~~. ~~In addition~~, the ~~plastic nature~~ of the ~~ligand-binding pockets in many nuclear receptors provides greater flexibility to further accommodate specific ligands with a variety~~ of ~~conformations~~. ~~Nuclear~~ receptor coactivators usually contain multiple LXXLL motifs that are used to interact with nuclear receptors. The nuclear receptors respond differently to distinct ligands and readily exchange their ligands in different environments. The conformational flexibility of the AF-2 helix allows the nuclear receptor to sense the presence of the bound ligands, either an agonist or an antagonist, and ~~to recruit~~ the ~~coactivators or corepressors that ultimately determine the transcriptional activation or repression~~ of ~~nuclear receptors~~.	+	Resistance to thyroid hormone (RTH) is a clinical disorder without specific and effective therapeutic strategy, partly due to the lack of structural mechanisms for the defective ligand binding by mutated thyroid hormone receptors (THRs). We herein uncovered the prescription drug roxadustat as a novel THRbeta-selective ligand with therapeutic potentials in treating RTH, thereby providing a small molecule tool enabling the first probe into the structural mechanisms of RTH. Despite a wide distribution of the receptor mutation sites, different THRbeta mutants induce allosteric conformational modulation on the same His435 residue, which disrupts a critical hydrogen bond required for the binding of thyroid hormones. Interestingly, roxadustat retains hydrophobic interactions with THRbeta via its unique phenyl extension, enabling the rescue of the activity of the THRbeta mutants. Our study thus reveals a critical receptor allosterism mechanism for RTH by mutant THRbeta, providing a new and viable therapeutic strategy for the treatment of RTH.

-	~~Structural and functional insights into nuclear receptor signaling~~.,~~Jin L~~, Li Y ~~Adv Drug Deliv Rev~~. ~~2010~~ Oct 30;~~62(13)~~:~~1218~~-26. doi: 10.1016/j.~~addr~~.~~2010~~.08.~~007~~. , Epub ~~2010 Aug 17~~. PMID:~~20723571~~<ref>PMID:~~20723571~~</ref>	+	Revealing a Mutant-Induced Receptor Allosteric Mechanism for the Thyroid Hormone Resistance.,Yao B, Wei Y, Zhang S, Tian S, Xu S, Wang R, Zheng W, Li Y iScience. 2019 Oct 25;20:489-496. doi: 10.1016/j.isci.2019.10.002. Epub 2019 Oct , 2. PMID:31655060<ref>PMID:31655060</ref>

	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>
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Li, Y]]		[[Category: Li, Y]]

OCA at 06:51, 23 October 2019

OCA — Wed, 23 Oct 2019 06:51:16 GMT

←Older revision		Revision as of 06:51, 23 October 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6kke is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==THRb mutation with a novel agonist==
		+	<StructureSection load='6kke' size='340' side='right'caption='[[6kke]], [[Resolution\|resolution]] 2.58Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6kke]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KKE FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8HO:2-[(1-methyl-4-oxidanyl-7-phenoxy-isoquinolin-3-yl)carbonylamino]ethanoic+acid'>8HO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6acm\|6acm]]</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=6kke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kke OCA], [http://pdbe.org/6kke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kke RCSB], [http://www.ebi.ac.uk/pdbsum/6kke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kke ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/THB_HUMAN THB_HUMAN]] Defects in THRB are the cause of generalized thyroid hormone resistance (GTHR) [MIM:[http://omim.org/entry/188570 188570]]. GTHR is a disease characterized by goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. GTHR patients also have high levels of circulating thyroid hormones (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH).<ref>PMID:2510172</ref> <ref>PMID:2153155</ref> <ref>PMID:1846005</ref> <ref>PMID:1661299</ref> <ref>PMID:1653889</ref> <ref>PMID:1563081</ref> <ref>PMID:1314846</ref> <ref>PMID:1619012</ref> <ref>PMID:1587388</ref> <ref>PMID:1324420</ref> <ref>PMID:8514853</ref> <ref>PMID:8175986</ref> <ref>PMID:7833659</ref> <ref>PMID:8664910</ref> <ref>PMID:8889584</ref> <ref>PMID:10660344</ref> <ref>PMID:16804041</ref> <ref>PMID:19268523</ref> Defects in THRB are the cause of generalized thyroid hormone resistance autosomal recessive (GTHRAR) [MIM:[http://omim.org/entry/274300 274300]]. An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone. Defects in THRB are the cause of selective pituitary thyroid hormone resistance (PRTH) [MIM:[http://omim.org/entry/145650 145650]]; also known as familial hyperthyroidism due to inappropriate thyrotropin secretion. PRTH is a variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established.<ref>PMID:7528740</ref> <ref>PMID:8381821</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/THB_HUMAN THB_HUMAN]] High affinity receptor for triiodothyronine.<ref>PMID:17418816</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Nuclear receptors are important transcriptional factors that share high sequence identity and conserved domains, including a DNA-binding domain (DBD) and a ligand-binding domain (LBD). The LBD plays a crucial role in ligand-mediated nuclear receptor activity. Hundreds of different crystal structures of nuclear receptors have revealed a general mechanism for the molecular basis of ligand binding and ligand-mediated regulation of nuclear receptors. Despite the conserved fold of nuclear receptor LBDs, the ligand-binding pocket is the least conserved region among different nuclear receptor LBDs. Structural comparison and analysis show that several features of the pocket, like the size and also the shape, have contributed to the ligand binding affinity and specificity. In addition, the plastic nature of the ligand-binding pockets in many nuclear receptors provides greater flexibility to further accommodate specific ligands with a variety of conformations. Nuclear receptor coactivators usually contain multiple LXXLL motifs that are used to interact with nuclear receptors. The nuclear receptors respond differently to distinct ligands and readily exchange their ligands in different environments. The conformational flexibility of the AF-2 helix allows the nuclear receptor to sense the presence of the bound ligands, either an agonist or an antagonist, and to recruit the coactivators or corepressors that ultimately determine the transcriptional activation or repression of nuclear receptors.

-	~~Authors: Yao, B.Q~~., Li, Y.	+	Structural and functional insights into nuclear receptor signaling.,Jin L, Li Y Adv Drug Deliv Rev. 2010 Oct 30;62(13):1218-26. doi: 10.1016/j.addr.2010.08.007. , Epub 2010 Aug 17. PMID:20723571<ref>PMID:20723571</ref>

-	~~Description: THRb mutation with~~ a ~~novel agonist~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	[[Category: ~~Yao, B.Q~~]]	+	<div class="pdbe-citations 6kke" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Li, Y]]		[[Category: Li, Y]]
		+	[[Category: Yao, B Q]]
		+	[[Category: Agonist]]
		+	[[Category: Anemia]]
		+	[[Category: Thyroid hormone receptor]]
		+	[[Category: Transcription]]

OCA at 14:54, 14 August 2019

OCA — Wed, 14 Aug 2019 14:54:22 GMT

←Older revision		Revision as of 14:54, 14 August 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6kke is ON HOLD	+	The entry 6kke is ON HOLD until Paper Publication

	Authors: Yao, B.Q., Li, Y.		Authors: Yao, B.Q., Li, Y.

OCA: Protected "6kke" [edit=sysop:move=sysop]

OCA — Wed, 31 Jul 2019 04:39:20 GMT

Protected "6kke" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:39, 31 July 2019

OCA: New page: '''Unreleased structure''' The entry 6kke is ON HOLD Authors: Yao, B.Q., Li, Y. Description: THRb mutation with a novel agonist Category: Unreleased Structures [[Category: Yao, B.Q...

OCA — Wed, 31 Jul 2019 04:39:19 GMT

New page: '''Unreleased structure''' The entry 6kke is ON HOLD Authors: Yao, B.Q., Li, Y. Description: THRb mutation with a novel agonist Category: Unreleased Structures [[Category: Yao, B.Q...

New page

'''Unreleased structure'''

The entry 6kke is ON HOLD

Authors: Yao, B.Q., Li, Y.

Description: THRb mutation with a novel agonist
[[Category: Unreleased Structures]]
[[Category: Yao, B.Q]]
[[Category: Li, Y]]