2fh2 - Revision history

OCA at 13:50, 13 March 2024

OCA — Wed, 13 Mar 2024 13:50:41 GMT

←Older revision		Revision as of 13:50, 13 March 2024
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	<StructureSection load='2fh2' size='340' side='right'caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2fh2' size='340' side='right'caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2fh2]] is a 3 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=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2fh2]] is a 3 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=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=CA:CALCIUM+ION'>CA</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]] 2.5Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [~~http~~://pdbe.org/2fh2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2fh2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2fh2 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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [https://pdbe.org/2fh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fh2 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/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/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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 22:		Line 22:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fh2 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fh2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Gelsolin is a calcium and pH-sensitive modulator of actin filament length. Here, we use X-ray crystallography to examine the extraction and exchange of calcium ions from their binding sites in different crystalline forms of the activated N and C-terminal halves of gelsolin, G1-G3 and G4-G6, respectively. We demonstrate that the combination of calcium and low pH activating conditions do not induce conformational changes in G4-G6 beyond those elicited by calcium alone. EGTA is able to remove calcium ions bound to the type I and type II metal ion-binding sites in G4-G6. Constrained by crystal contacts and stabilized by interdomain interaction surfaces, the gross structure of calcium-depleted G4-G6 remains that of the activated form. However, high-resolution details of changes in the ion-binding sites may represent the initial steps toward restoration of the arrangement of domains found in the calcium-free inactive form of gelsolin in solution. Furthermore, bathing crystals with the trivalent calcium ion mimic, Tb3+, results in anomalous scattering data that permit unequivocal localization of terbium ions in each of the proposed type I and type II ion-binding sites of both halves of gelsolin. In contrast to predictions based on solution studies, we find that no calcium ion is immune to exchange.
-
-	Calcium ion exchange in crystalline gelsolin.,Chumnarnsilpa S, Loonchanta A, Xue B, Choe H, Urosev D, Wang H, Lindberg U, Burtnick LD, Robinson RC J Mol Biol. 2006 Mar 31;357(3):773-82. Epub 2006 Jan 26. PMID:16466744<ref>PMID:16466744</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2fh2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[3D ~~Structures of gelsolin~~\|3D ~~Structures of gelsolin~~]]	+	*[[Gelsolin 3D structures\|Gelsolin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Burtnick~~, L D~~]]	+	[[Category: Burtnick LD]]
-	[[Category: Choe, H]]	+	[[Category: Choe H]]
-	[[Category: Chumnarnsilpa, S]]	+	[[Category: Chumnarnsilpa S]]
-	[[Category: Loonchanta, A]]	+	[[Category: Loonchanta A]]
-	[[Category: Robinson~~, R C~~]]	+	[[Category: Robinson RC]]
-	[[Category: Urosev, D]]	+	[[Category: Urosev D]]
-	[[Category: Wang, H]]	+	[[Category: Wang H]]
-	[[Category: Xue, B]]	+	[[Category: Xue B]]
-	~~[[Category: Contractile protein]]~~	+
-	~~[[Category: Egta]]~~	+
-	~~[[Category: Gelsolin~~]]	+

OCA at 11:07, 26 February 2020

OCA — Wed, 26 Feb 2020 11:07:50 GMT

←Older revision		Revision as of 11:07, 26 February 2020
Line 1:		Line 1:

	==C-terminal half of gelsolin soaked in EGTA at pH 4.5==		==C-terminal half of gelsolin soaked in EGTA at pH 4.5==
-	<StructureSection load='2fh2' size='340' side='right' caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='2fh2' size='340' side='right'caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fh2]] is a 3 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=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fh2]] is a 3 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=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[~~Gelsolin~~\|~~Gelsolin~~]]	+	*[[3D Structures of gelsolin\|3D Structures of gelsolin]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Burtnick, L D]]		[[Category: Burtnick, L D]]
	[[Category: Choe, H]]		[[Category: Choe, H]]

OCA at 07:32, 23 May 2018

OCA — Wed, 23 May 2018 07:32:24 GMT

←Older revision		Revision as of 07:32, 23 May 2018
Line 1:		Line 1:
		+
	==C-terminal half of gelsolin soaked in EGTA at pH 4.5==		==C-terminal half of gelsolin soaked in EGTA at pH 4.5==
	<StructureSection load='2fh2' size='340' side='right' caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2fh2' size='340' side='right' caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://pdbe.org/2fh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://pdbe.org/2fh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fh2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/2fh2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/2fh2_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fh2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 14:47, 11 September 2015

OCA — Fri, 11 Sep 2015 14:47:25 GMT

←Older revision		Revision as of 14:47, 11 September 2015
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	<StructureSection load='2fh2' size='340' side='right' caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2fh2' size='340' side='right' caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2fh2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2fh2]] is a 3 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=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://pdbe.org/2fh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 29:		Line 29:
	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 2fh2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Burtnick, L D]]		[[Category: Burtnick, L D]]
	[[Category: Choe, H]]		[[Category: Choe, H]]

OCA at 09:21, 16 January 2015

OCA — Fri, 16 Jan 2015 09:21:59 GMT

←Older revision		Revision as of 09:21, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fh2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fh2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 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>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Burtnick, L D.]]	+	[[Category: Burtnick, L D]]
-	[[Category: Choe, H.]]	+	[[Category: Choe, H]]
-	[[Category: Chumnarnsilpa, S.]]	+	[[Category: Chumnarnsilpa, S]]
-	[[Category: Loonchanta, A.]]	+	[[Category: Loonchanta, A]]
-	[[Category: Robinson, R C.]]	+	[[Category: Robinson, R C]]
-	[[Category: Urosev, D.]]	+	[[Category: Urosev, D]]
-	[[Category: Wang, H.]]	+	[[Category: Wang, H]]
-	[[Category: Xue, B.]]	+	[[Category: Xue, B]]
	[[Category: Contractile protein]]		[[Category: Contractile protein]]
	[[Category: Egta]]		[[Category: Egta]]
	[[Category: Gelsolin]]		[[Category: Gelsolin]]

OCA at 01:17, 30 September 2014

OCA — Tue, 30 Sep 2014 01:17:02 GMT

←Older revision		Revision as of 01:17, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2fh2\| PDB=2fh2 \| SCENE= }}~~	+	==C-terminal half of gelsolin soaked in EGTA at pH 4.5==
-	===C-terminal half of gelsolin soaked in EGTA at pH 4.5===	+	<StructureSection load='2fh2' size='340' side='right' caption='[[2fh2]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_16466744}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2fh2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fh1\|2fh1]], [[2fh3\|2fh3]], [[2fh4\|2fh4]]</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=2fh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fh2 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh2 PDBsum]</span></td></tr>
		+	<table>
		+	== 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>
		+	== Function ==
		+	[[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>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/2fh2_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Gelsolin is a calcium and pH-sensitive modulator of actin filament length. Here, we use X-ray crystallography to examine the extraction and exchange of calcium ions from their binding sites in different crystalline forms of the activated N and C-terminal halves of gelsolin, G1-G3 and G4-G6, respectively. We demonstrate that the combination of calcium and low pH activating conditions do not induce conformational changes in G4-G6 beyond those elicited by calcium alone. EGTA is able to remove calcium ions bound to the type I and type II metal ion-binding sites in G4-G6. Constrained by crystal contacts and stabilized by interdomain interaction surfaces, the gross structure of calcium-depleted G4-G6 remains that of the activated form. However, high-resolution details of changes in the ion-binding sites may represent the initial steps toward restoration of the arrangement of domains found in the calcium-free inactive form of gelsolin in solution. Furthermore, bathing crystals with the trivalent calcium ion mimic, Tb3+, results in anomalous scattering data that permit unequivocal localization of terbium ions in each of the proposed type I and type II ion-binding sites of both halves of gelsolin. In contrast to predictions based on solution studies, we find that no calcium ion is immune to exchange.

-	~~==Disease==~~	+	Calcium ion exchange in crystalline gelsolin.,Chumnarnsilpa S, Loonchanta A, Xue B, Choe H, Urosev D, Wang H, Lindberg U, Burtnick LD, Robinson RC J Mol Biol. 2006 Mar 31;357(3):773-82. Epub 2006 Jan 26. PMID:16466744<ref>PMID:16466744</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>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[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>
-		+
-	~~==About this Structure==~~	+
-	[[2fh2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA].	+

	==See Also==		==See Also==
	*[[Gelsolin\|Gelsolin]]		*[[Gelsolin\|Gelsolin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:016466744</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]

OCA at 20:08, 24 March 2013

OCA — Sun, 24 Mar 2013 20:08:14 GMT

←Older revision		Revision as of 20:08, 24 March 2013
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-	[[Image:2fh2.png\|left\|200px]]
-
	{{STRUCTURE_2fh2\| PDB=2fh2 \| SCENE= }}		{{STRUCTURE_2fh2\| PDB=2fh2 \| SCENE= }}
-
	===C-terminal half of gelsolin soaked in EGTA at pH 4.5===		===C-terminal half of gelsolin soaked in EGTA at pH 4.5===
		+	{{ABSTRACT_PUBMED_16466744}}

-	~~{{ABSTRACT_PUBMED_16466744}}~~	+	==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>
		+
		+	==Function==
		+	[[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>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:016466744</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016466744</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]

OCA at 19:41, 20 October 2012

OCA — Sat, 20 Oct 2012 19:41:53 GMT

←Older revision		Revision as of 19:41, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[2fh2]] is a 3 chain structure ~~of [[Gelsolin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA].	+	[[2fh2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH2 OCA].

	==See Also==		==See Also==

OCA at 08:11, 27 July 2012

OCA — Fri, 27 Jul 2012 08:11:09 GMT

←Older revision		Revision as of 08:11, 27 July 2012
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	[[Image:2fh2.png\|left\|200px]]		[[Image:2fh2.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2fh2", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2fh2\| PDB=2fh2 \| SCENE= }}		{{STRUCTURE_2fh2\| PDB=2fh2 \| SCENE= }}

	===C-terminal half of gelsolin soaked in EGTA at pH 4.5===		===C-terminal half of gelsolin soaked in EGTA at pH 4.5===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16466744}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16466744 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_16466744}}		{{ABSTRACT_PUBMED_16466744}}

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	==See Also==		==See Also==
-	*[[Gelsolin]]	+	*[[Gelsolin\|Gelsolin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16466744~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016466744</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]

OCA: Protected "2fh2" [edit=sysop:move=sysop]

OCA — Mon, 27 Dec 2010 01:50:33 GMT

Protected "2fh2" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:50, 27 December 2010