6sug - Revision history

OCA at 12:48, 24 January 2024

2024-01-24T12:48:32Z

←Older revision		Revision as of 12:48, 24 January 2024
Line 3:		Line 3:
	<StructureSection load='6sug' size='340' side='right'caption='[[6sug]], [[Resolution\|resolution]] 1.21Å' scene=''>		<StructureSection load='6sug' size='340' side='right'caption='[[6sug]], [[Resolution\|resolution]] 1.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6sug]] 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=6SUG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6SUG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6sug]] 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=6SUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SUG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=LVB:3~~-~~deoxytolcapone'>LVB</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]] 1.21Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~TTR, PALB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LVB:3-deoxytolcapone'>LVB</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6sug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sug OCA], [~~http~~://pdbe.org/6sug PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6sug RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6sug PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6sug 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=6sug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sug OCA], [https://pdbe.org/6sug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sug RCSB], [https://www.ebi.ac.uk/pdbsum/6sug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sug ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/TTHY_HUMAN TTHY_HUMAN]] Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR) [MIM:[~~http~~://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:[~~http~~://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:[~~http~~://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>	+	[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 ==		== Function ==
-	[~~[http~~://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>	+	[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 6sug" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6sug" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Transthyretin 3D structures\|Transthyretin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Berni, R]]	+	[[Category: Berni R]]
-	[[Category: Casnati, A]]	+	[[Category: Casnati A]]
-	[[Category: Cianci, M]]	+	[[Category: Cianci M]]
-	[[Category: Loconte, V]]	+	[[Category: Loconte V]]
-	[[Category: Menozzi, I]]	+	[[Category: Menozzi I]]
-	[[Category: Sansone, F]]	+	[[Category: Sansone F]]
-	[[Category: Sbravati, D]]	+	[[Category: Sbravati D]]
-	~~[[Category: Amyloidosis]]~~	+
-	~~[[Category: Binding protein]]~~	+
-	~~[[Category: Tetramer]]~~	+
-	~~[[Category: Transport protein~~]]	+

OCA at 11:29, 26 August 2020

2020-08-26T11:29:46Z

←Older revision		Revision as of 11:29, 26 August 2020
Line 1:		Line 1:

	==Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue==		==Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue==
-	<StructureSection load='6sug' size='340' side='right'caption='[[6sug]]' scene=''>	+	<StructureSection load='6sug' size='340' side='right'caption='[[6sug]], [[Resolution\|resolution]] 1.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SUG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6sug]] 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=6SUG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SUG FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sug OCA], [http://pdbe.org/6sug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sug RCSB], [http://www.ebi.ac.uk/pdbsum/6sug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sug ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LVB:3-deoxytolcapone'>LVB</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTR, PALB ([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://proteopedia.org/fgij/fg.htm?mol=6sug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sug OCA], [http://pdbe.org/6sug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sug RCSB], [http://www.ebi.ac.uk/pdbsum/6sug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sug ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/TTHY_HUMAN TTHY_HUMAN]] Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR) [MIM:[http://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:[http://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:[http://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 ==
		+	[[http://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 (TTR) is an amyloidogenic homotetramer involved in the transport of thyroxine and retinol in blood and cerebrospinal fluid. TTR stabilizers, such as tolcapone, an FDA approved drug for Parkinson's disease, are able to interact with residues of the thyroxine-binding sites of TTR, both wild type and pathogenic mutant forms, thereby stabilizing its tetrameric native state and inhibiting amyloidogenesis. Herein, we report on the synthesis of 3-deoxytolcapone, a novel stabilizer of TTR. The high-resolution X-ray analyses of the interactions of 3-O-methyltolcapone and 3-deoxytolcapone with TTR were performed. In the two TTR-ligand complexes the tolcapone analogues establish mainly H-bond and hydrophobic interactions with residues of the thyroxine-binding site of the TTR tetramer. Both compounds are capable of high and selective stabilization of TTR in the presence of plasma proteins, despite their markedly different 'forward' and 'reverse' binding mode, respectively. In fact, the loss or the weakening of stabilizing interactions with protein residues of 3-deoxytolcapone in comparison with tolcapone and 3-O-methyltolcapone is compensated by new interactions established at the dimer-dimer interface. Our data, coupled with previously reported data on the pharmacokinetics properties in humans of tolcapone and 3-O-methyltolcapone, further support the relevance of the latter tolcapone analogue as TTR stabilizer.
		+
		+	Interactions of tolcapone analogues as stabilizers of the amyloidogenic protein transthyretin.,Loconte V, Cianci M, Menozzi I, Sbravati D, Sansone F, Casnati A, Berni R Bioorg Chem. 2020 Jul 28;103:104144. doi: 10.1016/j.bioorg.2020.104144. PMID:32791384<ref>PMID:32791384</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6sug" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Berni R]]	+	[[Category: Berni, R]]
-	[[Category: Casnati A]]	+	[[Category: Casnati, A]]
-	[[Category: Cianci M]]	+	[[Category: Cianci, M]]
-	[[Category: Loconte V]]	+	[[Category: Loconte, V]]
-	[[Category: Menozzi I]]	+	[[Category: Menozzi, I]]
-	[[Category: Sansone F]]	+	[[Category: Sansone, F]]
-	[[Category: Sbravati D]]	+	[[Category: Sbravati, D]]
		+	[[Category: Amyloidosis]]
		+	[[Category: Binding protein]]
		+	[[Category: Tetramer]]
		+	[[Category: Transport protein]]

OCA at 05:32, 5 August 2020

2020-08-05T05:32:59Z

←Older revision		Revision as of 05:32, 5 August 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6sug ~~is ON HOLD until Paper Publication~~	+	==Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue==
-		+	<StructureSection load='6sug' size='340' side='right'caption='[[6sug]]' scene=''>
-	~~Authors~~: ~~Loconte, V~~.~~, Cianci, M~~., ~~Menozzi, I~~., ~~Sbravati, D~~., ~~Sansone, F~~., ~~Casnati, A~~., ~~Berni, R~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SUG FirstGlance]. <br>
-	~~Description: Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sug OCA], [http://pdbe.org/6sug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sug RCSB], [http://www.ebi.ac.uk/pdbsum/6sug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sug ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Sansone, F~~]]	+	__TOC__
-	[[Category: ~~Cianci, M~~]]	+	</StructureSection>
-	[[Category: ~~Menozzi, I~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Berni, R~~]]	+	[[Category: Berni R]]
-	[[Category: ~~Casnati, A~~]]	+	[[Category: Casnati A]]
-	[[Category: ~~Loconte, V~~]]	+	[[Category: Cianci M]]
-	[[Category: Sbravati, D]]	+	[[Category: Loconte V]]
		+	[[Category: Menozzi I]]
		+	[[Category: Sansone F]]
		+	[[Category: Sbravati D]]

OCA at 06:00, 22 July 2020

2020-07-22T06:00:28Z

←Older revision		Revision as of 06:00, 22 July 2020
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Loconte, V., Cianci, M., Menozzi, I., Sbravati, D., Sansone, F., Casnati, A., Berni, R.		Authors: Loconte, V., Cianci, M., Menozzi, I., Sbravati, D., Sansone, F., Casnati, A., Berni, R.
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	Description: Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue		Description: Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Berni, R]]
-	[[Category: Casnati, A]]
-	[[Category: Loconte, V]]
	[[Category: Sansone, F]]		[[Category: Sansone, F]]
	[[Category: Cianci, M]]		[[Category: Cianci, M]]
	[[Category: Menozzi, I]]		[[Category: Menozzi, I]]
		+	[[Category: Berni, R]]
		+	[[Category: Casnati, A]]
		+	[[Category: Loconte, V]]
	[[Category: Sbravati, D]]		[[Category: Sbravati, D]]

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

2019-10-02T07:49:16Z

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

←Older revision

Revision as of 07:49, 2 October 2019

OCA: New page: '''Unreleased structure''' The entry 6sug is ON HOLD Authors: Loconte, V., Cianci, M., Menozzi, I., Sbravati, D., Sansone, F., Casnati, A., Berni, R. Description: Crystal structure of ...

2019-10-02T07:49:15Z

New page: '''Unreleased structure''' The entry 6sug is ON HOLD Authors: Loconte, V., Cianci, M., Menozzi, I., Sbravati, D., Sansone, F., Casnati, A., Berni, R. Description: Crystal structure of ...

New page

'''Unreleased structure'''

The entry 6sug is ON HOLD

Authors: Loconte, V., Cianci, M., Menozzi, I., Sbravati, D., Sansone, F., Casnati, A., Berni, R.

Description: Crystal structure of transthyretin in complex with 3-deoxytolcapone, a tolcapone analogue
[[Category: Unreleased Structures]]
[[Category: Berni, R]]
[[Category: Casnati, A]]
[[Category: Loconte, V]]
[[Category: Sansone, F]]
[[Category: Cianci, M]]
[[Category: Menozzi, I]]
[[Category: Sbravati, D]]