4pkg - Revision history

OCA at 07:17, 27 September 2023

2023-09-27T07:17:42Z

← Older revision		Revision as of 07:17, 27 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PKG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PKG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [https://pdbe.org/4pkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [https://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg 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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [https://pdbe.org/4pkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [https://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg ProSAT]</span></td></tr>
	</table>		</table>

OCA at 13:10, 1 February 2023

2023-02-01T13:10:01Z

← Older revision		Revision as of 13:10, 1 February 2023
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	<StructureSection load='4pkg' size='340' side='right'caption='[[4pkg]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4pkg' size='340' side='right'caption='[[4pkg]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~] and [~~http~~://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4PKG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PKG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [https://pdbe.org/4pkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [https://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg ProSAT]</span></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</td></tr>~~
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TMOD1, D9S57E, TMOD ([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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [~~http~~://pdbe.org/4pkg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[~~[http~~://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[~~http~~://omim.org/entry/105120 105120]]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref> <ref>PMID:2153578</ref> <ref>PMID:2176481</ref> <ref>PMID:1338910</ref>		[https://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[https://omim.org/entry/105120 105120]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref> <ref>PMID:2153578</ref> <ref>PMID:2176481</ref> <ref>PMID:1338910</ref>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/~~ACTS_RABIT ACTS_RABIT~~]~~] Actins are highly conserved proteins that are involved~~ in ~~various types~~ of ~~cell motility and are ubiquitously expressed~~ in ~~all eukaryotic cells~~. [~~[http~~://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref>		[https://www.uniprot.org/uniprot/TMOD1_HUMAN TMOD1_HUMAN] Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus.<ref>PMID:8002995</ref> [https://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Dominguez, R]]		[[Category: Dominguez R]]
	[[Category: Rao~~, J N]]~~		[[Category: Rao JN]]
	~~[[Category: Actin filament]]~~
	~~[[Category: Actin-binding protein]]~~
	~~[[Category: Contractile protein]]~~
	~~[[Category: Contractile protein-actin-binding protein complex]]~~
	~~[[Category: Pointed-end capping protein]]~~
	~~[[Category: Tmod]]~~
	~~[[Category: Tropomyosin~~]]

OCA at 07:35, 17 April 2019

2019-04-17T07:35:46Z

← Older revision		Revision as of 07:35, 17 April 2019
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	==Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin==		==Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin==
	<StructureSection load='4pkg' size='340' side='right' caption='[[4pkg]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4pkg' size='340' side='right'caption='[[4pkg]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TMOD1, D9S57E, TMOD ([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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [http://pdbe.org/4pkg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [http://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg 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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [http://pdbe.org/4pkg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [http://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg ProSAT]</span></td></tr>
	</table>		</table>
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	==See Also==		==See Also==
	*[[Actin\|Actin]]		*[[Actin 3D structures\|Actin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Dominguez, R]]		[[Category: Dominguez, R]]

OCA at 10:05, 11 August 2016

2016-08-11T10:05:54Z

← Older revision		Revision as of 10:05, 11 August 2016
Line 1:		Line 1:

	==Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin==		==Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin==
	<StructureSection load='4pkg' size='340' side='right' caption='[[4pkg]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4pkg' size='340' side='right' caption='[[4pkg]], [[Resolution\|resolution]] 1.80Å' scene=''>
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	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [http://www.ebi.ac.uk/pdbsum/4pkg 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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [http://pdbe.org/4pkg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [http://www.ebi.ac.uk/pdbsum/4pkg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pkg ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 4pkg" style="background-color:#fffaf0;"></div>

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

OCA at 14:28, 5 January 2015

2015-01-05T14:28:21Z

← Older revision		Revision as of 14:28, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKG FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4pkh\|4pkh]], [[4pki\|4pki]]</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [http://www.ebi.ac.uk/pdbsum/4pkg 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=4pkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pkg RCSB], [http://www.ebi.ac.uk/pdbsum/4pkg PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[http://omim.org/entry/105120 105120]]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref> <ref>PMID:2153578</ref> <ref>PMID:2176481</ref> <ref>PMID:1338910</ref>		[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[http://omim.org/entry/105120 105120]]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref> <ref>PMID:2153578</ref> <ref>PMID:2176481</ref> <ref>PMID:1338910</ref>
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	</StructureSection>		</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Dominguez, R.]]		[[Category: Dominguez, R]]
	[[Category: Rao, J N.]]		[[Category: Rao, J N]]
	[[Category: Actin filament]]		[[Category: Actin filament]]
	[[Category: Actin-binding protein]]		[[Category: Actin-binding protein]]

OCA at 02:24, 7 August 2014

2014-08-07T02:24:19Z

← Older revision		Revision as of 02:24, 7 August 2014
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	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref>		[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Proteins that cap the ends of the actin filament are essential regulators of cytoskeleton dynamics. Whereas several proteins cap the rapidly growing barbed end, tropomodulin (Tmod) is the only protein known to cap the slowly growing pointed end. The lack of structural information severely limits our understanding of Tmod's capping mechanism. We describe crystal structures of actin complexes with the unstructured amino-terminal and the leucine-rich repeat carboxy-terminal domains of Tmod. The structures and biochemical analysis of structure-inspired mutants showed that one Tmod molecule interacts with three actin subunits at the pointed end, while also contacting two tropomyosin molecules on each side of the filament. We found that Tmod achieves high-affinity binding through several discrete low-affinity interactions, which suggests a mechanism for controlled subunit exchange at the pointed end.

			Actin cytoskeleton. Mechanism of actin filament pointed-end capping by tropomodulin.,Rao JN, Madasu Y, Dominguez R Science. 2014 Jul 25;345(6195):463-7. doi: 10.1126/science.1256159. PMID:25061212<ref>PMID:25061212</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:51, 30 July 2014

2014-07-30T07:51:11Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin==
+<StructureSection load='4pkg' size='340' side='right' caption='[[4pkg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-The entry 4pkg is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKG FirstGlance]. <br>
-Authors: Rao, J.N., Dominguez, R.
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
-Description: Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pkh|4pkh]], [[4pki|4pki]]</td></tr>

OCA at 06:43, 9 July 2014

2014-07-09T06:43:31Z

← Older revision		Revision as of 06:43, 9 July 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4pkg is ON HOLD		The entry 4pkg is ON HOLD until Paper Publication

	Authors: Rao, J.N., Dominguez, R.		Authors: Rao, J.N., Dominguez, R.

	Description: Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin		Description: Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin

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

2014-05-21T08:07:45Z

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

← Older revision	Revision as of 08:07, 21 May 2014
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4pkg is ON HOLD Authors: Rao, J.N., Dominguez, R. Description: Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin

2014-05-21T08:07:43Z

New page: '''Unreleased structure''' The entry 4pkg is ON HOLD Authors: Rao, J.N., Dominguez, R. Description: Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin

New page

'''Unreleased structure'''

The entry 4pkg is ON HOLD

Authors: Rao, J.N., Dominguez, R.

Description: Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin