4tng - Revision history

OCA at 00:46, 28 December 2023

OCA — Thu, 28 Dec 2023 00:46:59 GMT

←Older revision		Revision as of 00:46, 28 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4tng]] 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=4TNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TNG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4tng]] 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=4TNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TNG 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=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [https://pdbe.org/4tng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [https://www.ebi.ac.uk/pdbsum/4tng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tng 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]] 1.6Å</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=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [https://pdbe.org/4tng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [https://www.ebi.ac.uk/pdbsum/4tng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tng ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 10:46, 15 March 2023

OCA — Wed, 15 Mar 2023 10:46:51 GMT

←Older revision		Revision as of 10:46, 15 March 2023
Line 1:		Line 1:

	==Crystal Structure of Human Transthyretin Thr119Met Mutant==		==Crystal Structure of Human Transthyretin Thr119Met Mutant==
-	<StructureSection load='4tng' size='340' side='right' caption='[[4tng]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='4tng' size='340' side='right'caption='[[4tng]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4tng]] 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=4TNG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4TNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4tng]] 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=4TNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TNG FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4tkw\|4tkw]], [[4tl4\|4tl4]], [[4tl5\|4tl5]], [[4tlk\|4tlk]], [[4tls\|4tls]], [[4tlt\|4tlt]], [[4tlu\|4tlu]], [[4tm9\|4tm9]], [[4tne\|4tne]], [[4tnf\|4tnf]]</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=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [https://pdbe.org/4tng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [https://www.ebi.ac.uk/pdbsum/4tng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tng ProSAT]</span></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~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [~~http~~://pdbe.org/4tng PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4tng PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4tng 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>
		+
		+	==See Also==
		+	*[[Transthyretin 3D structures\|Transthyretin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Cascio, D~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Eisenberg,~~ D S]]	+	[[Category: Cascio D]]
-	[[Category: ~~Saelices, L~~]]	+	[[Category: Eisenberg DS]]
-	[[Category: ~~Sawaya, M~~]]	+	[[Category: Saelices L]]
-	[[Category: ~~Amyloid]]~~	+	[[Category: Sawaya M]]
-	~~[[Category: Human transthyretin]]~~	+
-	~~[[Category: Mutant]]~~	+
-	~~[[Category: Transport protein]]~~	+
-	~~[[Category: Transthyretin~~]]	+

OCA at 09:15, 22 November 2017

OCA — Wed, 22 Nov 2017 09:15:40 GMT

←Older revision		Revision as of 09:15, 22 November 2017
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		+
	==Crystal Structure of Human Transthyretin Thr119Met Mutant==		==Crystal Structure of Human Transthyretin Thr119Met Mutant==
	<StructureSection load='4tng' size='340' side='right' caption='[[4tng]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4tng' size='340' side='right' caption='[[4tng]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4tng]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4tng]] 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=4TNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TNG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4tkw\|4tkw]], [[4tl4\|4tl4]], [[4tl5\|4tl5]], [[4tlk\|4tlk]], [[4tls\|4tls]], [[4tlt\|4tlt]], [[4tlu\|4tlu]], [[4tm9\|4tm9]], [[4tne\|4tne]], [[4tnf\|4tnf]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4tkw\|4tkw]], [[4tl4\|4tl4]], [[4tl5\|4tl5]], [[4tlk\|4tlk]], [[4tls\|4tls]], [[4tlt\|4tlt]], [[4tlu\|4tlu]], [[4tm9\|4tm9]], [[4tne\|4tne]], [[4tnf\|4tnf]]</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=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [http://pdbe.org/4tng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [http://www.ebi.ac.uk/pdbsum/4tng PDBsum]</span></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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [http://pdbe.org/4tng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [http://www.ebi.ac.uk/pdbsum/4tng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tng ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 14:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]
	[[Category: Eisenberg, D S]]		[[Category: Eisenberg, D S]]

OCA at 19:34, 30 December 2015

OCA — Wed, 30 Dec 2015 19:34:38 GMT

←Older revision		Revision as of 19:34, 30 December 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal Structure of Human Transthyretin Thr119Met Mutant==
-		+	<StructureSection load='4tng' size='340' side='right' caption='[[4tng]], [[Resolution\|resolution]] 1.60Å' scene=''>
-	~~The entry~~ 4tng is ~~ON HOLD until Dec 30 2016~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4tng]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TNG FirstGlance]. <br>
-	~~Authors~~: ~~Saelices~~, L., ~~Cascio~~, D., ~~Sawaya~~, M., ~~Eisenberg~~, D.S.	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4tkw\|4tkw]], [[4tl4\|4tl4]], [[4tl5\|4tl5]], [[4tlk\|4tlk]], [[4tls\|4tls]], [[4tlt\|4tlt]], [[4tlu\|4tlu]], [[4tm9\|4tm9]], [[4tne\|4tne]], [[4tnf\|4tnf]]</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=4tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tng OCA], [http://pdbe.org/4tng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tng RCSB], [http://www.ebi.ac.uk/pdbsum/4tng PDBsum]</span></td></tr>
-	~~Description: Crystal Structure of Human Transthyretin Thr119Met Mutant~~	+	</table>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	== Disease ==
-	[[~~Category~~: ~~Sawaya, M~~]]	+	[[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>
-	[[~~Category~~: ~~Eisenberg~~, D.S]]	+	== Function ==
-	[[~~Category~~: ~~Saelices, L~~]]	+	[[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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Cascio, D]]		[[Category: Cascio, D]]
		+	[[Category: Eisenberg, D S]]
		+	[[Category: Saelices, L]]
		+	[[Category: Sawaya, M]]
		+	[[Category: Amyloid]]
		+	[[Category: Human transthyretin]]
		+	[[Category: Mutant]]
		+	[[Category: Transport protein]]
		+	[[Category: Transthyretin]]

OCA at 08:59, 6 May 2015

OCA — Wed, 06 May 2015 08:59:01 GMT

←Older revision		Revision as of 08:59, 6 May 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4tng is ON HOLD until ~~Paper Publication~~	+	The entry 4tng is ON HOLD until Dec 30 2016

	Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S.		Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S.

OCA at 17:44, 24 December 2014

OCA — Wed, 24 Dec 2014 17:44:22 GMT

←Older revision		Revision as of 17:44, 24 December 2014
Line 6:		Line 6:

	Description: Crystal Structure of Human Transthyretin Thr119Met Mutant		Description: Crystal Structure of Human Transthyretin Thr119Met Mutant
		+	[[Category: Unreleased Structures]]
		+	[[Category: Sawaya, M]]
		+	[[Category: Eisenberg, D.S]]
		+	[[Category: Saelices, L]]
		+	[[Category: Cascio, D]]

OCA at 09:53, 16 July 2014

OCA — Wed, 16 Jul 2014 09:53:15 GMT

←Older revision		Revision as of 09:53, 16 July 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S.		Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S.

	Description: Crystal Structure of Human Transthyretin Thr119Met Mutant		Description: Crystal Structure of Human Transthyretin Thr119Met Mutant

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

OCA — Wed, 11 Jun 2014 08:14:41 GMT

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

←Older revision

Revision as of 08:14, 11 June 2014

OCA: New page: '''Unreleased structure''' The entry 4tng is ON HOLD Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S. Description: Crystal Structure of Human Transthyretin Thr119Met Muta...

OCA — Wed, 11 Jun 2014 08:14:40 GMT

New page: '''Unreleased structure''' The entry 4tng is ON HOLD Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S. Description: Crystal Structure of Human Transthyretin Thr119Met Muta...

New page

'''Unreleased structure'''

The entry 4tng is ON HOLD

Authors: Saelices, L., Cascio, D., Sawaya, M., Eisenberg, D.S.

Description: Crystal Structure of Human Transthyretin Thr119Met Mutant