Tdp-43 - Revision history

Gerry Lushington at 21:36, 17 March 2018

Gerry Lushington — Sat, 17 Mar 2018 21:36:06 GMT

←Older revision		Revision as of 21:36, 17 March 2018
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	TDP-43 helical stabilizers		TDP-43 helical stabilizers
-	<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>	+	<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3037571/)' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils.

Michal Harel at 08:19, 2 January 2018

Michal Harel — Tue, 02 Jan 2018 08:19:13 GMT

←Older revision		Revision as of 08:19, 2 January 2018
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	TDP-43 helical stabilizers		TDP-43 helical stabilizers
	<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>		<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>
-	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils~~. '''Tdp-43'''~~.	+	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils.


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	Tdp-43 mutations were found ion familial and sporadic ALS patients<ref>PMID:18309045</ref>. Phosphorylated Tdp-43 is deposited as cytoplasmic and intranuclear inclusions in brains of patients with frontotemporal lobar degeneration and ALS<ref>PMID:18546284</ref>.		Tdp-43 mutations were found ion familial and sporadic ALS patients<ref>PMID:18309045</ref>. Phosphorylated Tdp-43 is deposited as cytoplasmic and intranuclear inclusions in brains of patients with frontotemporal lobar degeneration and ALS<ref>PMID:18546284</ref>.
-
-	== Relevance ==

	== Structural highlights ==		== Structural highlights ==

Michal Harel at 08:11, 2 January 2018

Michal Harel — Tue, 02 Jan 2018 08:11:37 GMT

←Older revision		Revision as of 08:11, 2 January 2018
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	== Disease ==		== Disease ==
		+
		+	Tdp-43 mutations were found ion familial and sporadic ALS patients<ref>PMID:18309045</ref>. Phosphorylated Tdp-43 is deposited as cytoplasmic and intranuclear inclusions in brains of patients with frontotemporal lobar degeneration and ALS<ref>PMID:18546284</ref>.

	== Relevance ==		== Relevance ==
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	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.
	</StructureSection>		</StructureSection>
		+
		+	== 3D Structures of Tdp-43 ==
		+
		+	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
		+
		+	[[2cqg]] – hTDP-43 RRM1 domain – human - NMR <br />
		+	[[1wf0]] – hTDP-43 RRM2 domain - NMR <br />
		+	[[5mrg]], [[2n4p]], [[5x4f]] – hTDP-43 N-terminal domain - NMR <br />
		+	[[5mdi]] – hTDP-43 N-terminal domain <br />
		+	[[2n2c]], [[2n3x]] – hTDP-43 prion-like helix - NMR <br />
		+	[[2n4g]], [[2n4h]] – hTDP-43 prion-like helix (mutant) - NMR <br />
		+	[[4y0f]], [[4iuf]] – hTDP-43 RRM1 domain + DNA <br />
		+	[[4y00]] – hTDP-43 RRM1 domain (mutant) + DNA <br />
		+	[[4bs2]] – hTDP-43 RRM1+RRM2 domains + RNA - NMR<br />
		+	[[3d2w]] – TDP-43 RRM2 domain + DNA - mouse<br />
		+
	== References ==		== References ==
	<references/>		<references/>

Michal Harel at 07:59, 2 January 2018

Michal Harel — Tue, 02 Jan 2018 07:59:18 GMT

←Older revision		Revision as of 07:59, 2 January 2018
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	TDP-43 helical stabilizers		TDP-43 helical stabilizers
	<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>		<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>
-	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''~~. Click above on '''edit this page''' to modify. Be careful with the < and > signs~~.	+	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''.
-	~~You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.~~	+

	== Function ==		== Function ==
		+
		+	'''Tdp-43''' or '''TAR DNA-binding protein 43''' is a heterogeneous nuclear ribonucleoprotein which has crucial roles in gene expression and alternative splicing, stress response, neuronal functions such as neurite outgrowth and many other cellular processes<ref>PMID:17981595</ref>.

	== Disease ==		== Disease ==
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	== Structural highlights ==		== Structural highlights ==

-	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. ~~You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.~~	+	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.
-		+
	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Michal Harel at 15:47, 12 January 2017

Michal Harel — Thu, 12 Jan 2017 15:47:19 GMT

←Older revision		Revision as of 15:47, 12 January 2017
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	TDP-43 helical stabilizers		TDP-43 helical stabilizers
-	<StructureSection load='2n2cligalza0.pdb.gz' size='~~600~~' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>	+	<StructureSection load='2n2cligalza0.pdb.gz' size='350' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Gerry Lushington at 16:05, 3 March 2016

Gerry Lushington — Thu, 03 Mar 2016 16:05:30 GMT

←Older revision		Revision as of 16:05, 3 March 2016
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	TDP-43 helical stabilizers		TDP-43 helical stabilizers
-	<StructureSection load='2n2cligalza0.pdb.gz' size='~~340~~' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>	+	<StructureSection load='2n2cligalza0.pdb.gz' size='600' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Gerry Lushington at 15:07, 3 March 2016

Gerry Lushington — Thu, 03 Mar 2016 15:07:36 GMT

←Older revision		Revision as of 15:07, 3 March 2016
Line 1:		Line 1:
	TDP-43 helical stabilizers		TDP-43 helical stabilizers
-	<StructureSection load='~~2n2c_ligalza0~~.pdb' size='340' side='right' caption='~~Caption for this structure~~' scene=''>	+	<StructureSection load='2n2cligalza0.pdb.gz' size='340' side='right' caption='Compound A is the best current binder to the healthy helical tdp-43' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Gerry Lushington at 14:57, 3 March 2016

Gerry Lushington — Thu, 03 Mar 2016 14:57:42 GMT

←Older revision		Revision as of 14:57, 3 March 2016
Line 1:		Line 1:
	TDP-43 helical stabilizers		TDP-43 helical stabilizers
-	<StructureSection load='2n2c_ligalza0.pdb~~.gz~~' size='340' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='2n2c_ligalza0.pdb' size='340' side='right' caption='Caption for this structure' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Gerry Lushington at 14:57, 3 March 2016

Gerry Lushington — Thu, 03 Mar 2016 14:57:05 GMT

←Older revision		Revision as of 14:57, 3 March 2016
Line 1:		Line 1:
-	~~<Structure load='2n2c_ligalza0.pdb' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />~~TDP-43 helical stabilizers	+	TDP-43 helical stabilizers
-	<StructureSection load='~~1stp~~' size='340' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='2n2c_ligalza0.pdb.gz' size='340' side='right' caption='Caption for this structure' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Gerry Lushington at 14:52, 3 March 2016

Gerry Lushington — Thu, 03 Mar 2016 14:52:40 GMT

←Older revision		Revision as of 14:52, 3 March 2016
Line 1:		Line 1:
-	<Structure load='2n2c_ligalza0.pdb~~.gz~~' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />TDP-43 helical stabilizers	+	<Structure load='2n2c_ligalza0.pdb' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />TDP-43 helical stabilizers
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
	This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is the healthy helical coil (residues 307-349) of TDP-43. A key biomolecular cause of ALS appears to be a helix-sheet transition in this area, leading to the formation of protein fibrils. '''Tdp-43'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.