OCA at 19:54, 29 May 2024

OCA — Wed, 29 May 2024 19:54:09 GMT

←Older revision		Revision as of 19:54, 29 May 2024
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	</div>		</div>
	<div class="pdbe-citations 8ii3" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 8ii3" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Transthyretin 3D structures\|Transthyretin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:21, 28 June 2023

OCA — Wed, 28 Jun 2023 21:21:00 GMT

←Older revision		Revision as of 21:21, 28 June 2023
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-	'''Unreleased structure'''

-	The entry ~~8ii3~~ is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of V30M-TTR in complex with 6-hydroxy BID==
		+	<StructureSection load='8ii3' size='340' side='right'caption='[[8ii3]], [[Resolution\|resolution]] 1.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8ii3]] 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=8II3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8II3 FirstGlance]. <br>
		+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.399Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PKK:[3,5-bis(iodanyl)-4-oxidanyl-phenyl]-(2-ethyl-6-oxidanyl-1-benzofuran-3-yl)methanone'>PKK</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=8ii3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ii3 OCA], [https://pdbe.org/8ii3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ii3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ii3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ii3 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/TTHY_HUMAN TTHY_HUMAN] Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR) [MIM:[https://omim.org/entry/105210 105210]. A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor.<ref>PMID:11243784</ref> <ref>PMID:15735344</ref> <ref>PMID:19167329</ref> <ref>PMID:3818577</ref> <ref>PMID:3022108</ref> <ref>PMID:6651852</ref> <ref>PMID:6583672</ref> <ref>PMID:3135807</ref> <ref>PMID:1517749</ref> <ref>PMID:1932142</ref> <ref>PMID:7923855</ref> <ref>PMID:8382610</ref> <ref>PMID:8428915</ref> <ref>PMID:9733771</ref> <ref>PMID:12403615</ref> <ref>PMID:16185074</ref> <ref>PMID:16627944</ref> <ref>PMID:6487335</ref> <ref>PMID:3722385</ref> <ref>PMID:2891727</ref> <ref>PMID:2161654</ref> <ref>PMID:2363717</ref> <ref>PMID:1656975</ref> <ref>PMID:2046936</ref> <ref>PMID:1570831</ref> <ref>PMID:1734866</ref> <ref>PMID:1520326</ref> <ref>PMID:1520336</ref> <ref>PMID:1544214</ref> <ref>PMID:1351039</ref> <ref>PMID:1301926</ref> <ref>PMID:1362222</ref> <ref>PMID:1436517</ref> <ref>PMID:8352764</ref> <ref>PMID:8038017</ref> <ref>PMID:8257997</ref> <ref>PMID:8095302</ref> <ref>PMID:1997217</ref> <ref>PMID:8019560</ref> <ref>PMID:8081397</ref> <ref>PMID:7914929</ref> <ref>PMID:8133316</ref> <ref>PMID:7910950</ref> <ref>PMID:7655883</ref> <ref>PMID:7850982</ref> <ref>PMID:8579098</ref> <ref>PMID:9066351</ref> <ref>PMID:8990019</ref> <ref>PMID:9605286</ref> <ref>PMID:10036587</ref> <ref>PMID:10627135</ref> <ref>PMID:10694917</ref> <ref>PMID:10211412</ref> <ref>PMID:10439117</ref> <ref>PMID:10611950</ref> <ref>PMID:10071047</ref> <ref>PMID:10436378</ref> <ref>PMID:10842705</ref> <ref>PMID:10842718</ref> <ref>PMID:10882995</ref> <ref>PMID:11445644</ref> <ref>PMID:12557757</ref> <ref>PMID:11866053</ref> <ref>PMID:12050338</ref> <ref>PMID:12771253</ref> <ref>PMID:15214015</ref> <ref>PMID:15478468</ref> <ref>PMID:15217993</ref> <ref>PMID:17453626</ref> <ref>PMID:17577687</ref> <ref>PMID:17503405</ref> <ref>PMID:17635579</ref> Defects in TTR are a cause of hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE) [MIM:[https://omim.org/entry/145680 145680]. It is a condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities.<ref>PMID:1979335</ref> Defects in TTR are a cause of carpal tunnel syndrome type 1 (CTS1) [MIM:[https://omim.org/entry/115430 115430]. It is a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis.<ref>PMID:8309582</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/TTHY_HUMAN TTHY_HUMAN] Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.<ref>PMID:3714052</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Transthyretin amyloidosis is a progressive systemic disorder that is caused by the amyloid deposition of transthyretin in various organs. Stabilization of the native transthyretin is an effective strategy for the treatment of transthyretin amyloidosis. In this study we demonstrate that the clinically used uricosuric agent benziodarone is highly effective to stabilize the tetrameric structure of transthyretin. An acid-induced aggregation assay showed that benziodarone had strong inhibitory activity similar to that of tafamidis, which is currently used as a therapeutic agent for transthyretin amyloidosis. Moreover, a possible metabolite, 6-hydroxybenziodarone, retained the strong amyloid inhibitory activity of benziodarone. An ex vivo competitive binding assay using a fluorogenic probe showed that benziodarone and 6-hydroxybenziodarone were highly potent for selective binding to transthyretin in human plasma. An X-ray crystal structure analysis revealed that the halogenated hydroxyphenyl ring was located at the entrance of the thyroxine binding channel of transthyretin and that the benzofuran ring was located in the inner channel. These studies suggest that benziodarone and 6-hydroxybenziodarone would potentially be effective against transthyretin amyloidosis.

-	~~Authors:~~ Yokoyama, T.	+	Benziodarone and 6-hydroxybenziodarone are potent and selective inhibitors of transthyretin amyloidogenesis.,Mizuguchi M, Yokoyama T, Okada T, Nakagawa Y, Fujii K, Nabeshima Y, Toyooka N Bioorg Med Chem. 2023 Jul 15;90:117370. doi: 10.1016/j.bmc.2023.117370. Epub 2023 , Jun 9. PMID:37311373<ref>PMID:37311373</ref>

-	~~Description: Crystal structure~~ of ~~V30M~~-~~TTR in complex with 6~~-~~hydroxy BID~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: Yokoyama, T]]	+	<div class="pdbe-citations 8ii3" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Yokoyama T]]

OCA at 18:42, 12 April 2023

OCA — Wed, 12 Apr 2023 18:42:05 GMT

←Older revision		Revision as of 18:42, 12 April 2023
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8ii3 is ON HOLD	+	The entry 8ii3 is ON HOLD until Paper Publication

	Authors: Yokoyama, T.		Authors: Yokoyama, T.

OCA: Protected "8ii3" [edit=sysop:move=sysop]

OCA — Thu, 02 Mar 2023 04:44:33 GMT

Protected "8ii3" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:44, 2 March 2023

OCA: New page: '''Unreleased structure''' The entry 8ii3 is ON HOLD Authors: Yokoyama, T. Description: Crystal structure of V30M-TTR in complex with 6-hydroxy BID Category: Unreleased Structures ...

OCA — Thu, 02 Mar 2023 04:44:32 GMT

New page: '''Unreleased structure''' The entry 8ii3 is ON HOLD Authors: Yokoyama, T. Description: Crystal structure of V30M-TTR in complex with 6-hydroxy BID Category: Unreleased Structures ...

New page

'''Unreleased structure'''

The entry 8ii3 is ON HOLD

Authors: Yokoyama, T.

Description: Crystal structure of V30M-TTR in complex with 6-hydroxy BID
[[Category: Unreleased Structures]]
[[Category: Yokoyama, T]]

8ii3 - Revision history

OCA at 19:54, 29 May 2024

OCA at 21:21, 28 June 2023

OCA at 18:42, 12 April 2023

OCA: Protected "8ii3" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 8ii3 is ON HOLD Authors: Yokoyama, T. Description: Crystal structure of V30M-TTR in complex with 6-hydroxy BID Category: Unreleased Structures ...