4qrf - Revision history

OCA at 15:09, 8 November 2023

2023-11-08T15:09:13Z

← Older revision		Revision as of 15:09, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qrf]] 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=4QRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qrf]] 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=4QRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</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]] 1.8Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [https://pdbe.org/4qrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [https://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf 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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [https://pdbe.org/4qrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [https://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf ProSAT]</span></td></tr>
	</table>		</table>

OCA at 13:48, 22 February 2023

2023-02-22T13:48:43Z

← Older revision		Revision as of 13:48, 22 February 2023
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	<StructureSection load='4qrf' size='340' side='right'caption='[[4qrf]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4qrf' size='340' side='right'caption='[[4qrf]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qrf]] 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=4QRF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4QRF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qrf]] 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=4QRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pwe\|4pwe]], [[4pwf\|4pwf]], [[4pwg\|4pwg]], [[4pwh\|4pwh]], [[4pwi\|4pwi]], [[4pwj\|4pwj]]</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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [https://pdbe.org/4qrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [https://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf 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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [~~http~~://pdbe.org/4qrf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf 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 ==
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	==See Also==		==See Also==
	*[[Transthyretin\|Transthyretin]]		*[[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: Kosaka, Y]]		[[Category: Kosaka Y]]
	[[Category: Mizuguchi, M]]		[[Category: Mizuguchi M]]
	[[Category: Yokoyama, T]]		[[Category: Yokoyama T]]
	~~[[Category: Thyroxine binding]]~~
	~~[[Category: Transport protein]]~~
	~~[[Category: Transporter~~]]

OCA at 08:42, 24 April 2019

2019-04-24T08:42:36Z

← Older revision		Revision as of 08:42, 24 April 2019
Line 1:		Line 1:

	==Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester==		==Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester==
	<StructureSection load='4qrf' size='340' side='right' caption='[[4qrf]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4qrf' size='340' side='right'caption='[[4qrf]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qrf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qrf]] 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=4QRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pwe\|4pwe]], [[4pwf\|4pwf]], [[4pwg\|4pwg]], [[4pwh\|4pwh]], [[4pwi\|4pwi]], [[4pwj\|4pwj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pwe\|4pwe]], [[4pwf\|4pwf]], [[4pwg\|4pwg]], [[4pwh\|4pwh]], [[4pwi\|4pwi]], [[4pwj\|4pwj]]</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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [http://pdbe.org/4qrf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [http://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf 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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [http://pdbe.org/4qrf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [http://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf ProSAT]</span></td></tr>
	</table>		</table>
Line 28:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Kosaka, Y]]		[[Category: Kosaka, Y]]
	[[Category: Mizuguchi, M]]		[[Category: Mizuguchi, M]]

OCA at 17:45, 11 August 2016

2016-08-11T17:45:56Z

← Older revision		Revision as of 17:45, 11 August 2016
Line 1:		Line 1:

	==Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester==		==Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester==
	<StructureSection load='4qrf' size='340' side='right' caption='[[4qrf]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4qrf' size='340' side='right' caption='[[4qrf]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QAP:2-PHENYLETHYL+(2E)-3-(3,4-DIHYDROXYPHENYL)PROP-2-ENOATE'>QAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pwe\|4pwe]], [[4pwf\|4pwf]], [[4pwg\|4pwg]], [[4pwh\|4pwh]], [[4pwi\|4pwi]], [[4pwj\|4pwj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pwe\|4pwe]], [[4pwf\|4pwf]], [[4pwg\|4pwg]], [[4pwh\|4pwh]], [[4pwi\|4pwi]], [[4pwj\|4pwj]]</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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [http://www.ebi.ac.uk/pdbsum/4qrf 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=4qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrf OCA], [http://pdbe.org/4qrf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qrf RCSB], [http://www.ebi.ac.uk/pdbsum/4qrf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 4qrf" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Transthyretin\|Transthyretin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:55, 26 November 2014

2014-11-26T07:55:04Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester==
-The entry 4qrf is ON HOLD
+Inhibitory Activities of Propolis and Its Promising Component, Caffeic Acid Phenethyl Ester, against Amyloidogenesis of Human Transthyretin.,Yokoyama T, Kosaka Y, Mizuguchi M J Med Chem. 2014 Nov 13;57(21):8928-35. doi: 10.1021/jm500997m. Epub 2014 Oct 20. PMID:25314129<ref>PMID:25314129</ref>
-Authors: Yokoyama, T., Kosaka, Y., Mizuguchi, M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester
+== References ==

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

2014-07-09T06:53:12Z

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

← Older revision	Revision as of 06:53, 9 July 2014
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OCA: New page: '''Unreleased structure''' The entry 4qrf is ON HOLD Authors: Yokoyama, T., Kosaka, Y., Mizuguchi, M. Description: Crystal structure of V30M mutant human transthyretin complexed with c...

2014-07-09T06:53:12Z

New page: '''Unreleased structure''' The entry 4qrf is ON HOLD Authors: Yokoyama, T., Kosaka, Y., Mizuguchi, M. Description: Crystal structure of V30M mutant human transthyretin complexed with c...

New page

'''Unreleased structure'''

The entry 4qrf is ON HOLD

Authors: Yokoyama, T., Kosaka, Y., Mizuguchi, M.

Description: Crystal structure of V30M mutant human transthyretin complexed with caffeic acid phenethyl ester