3ffn - Revision history

OCA at 09:49, 21 February 2024

OCA — Wed, 21 Feb 2024 09:49:15 GMT

←Older revision		Revision as of 09:49, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3ffn' size='340' side='right'caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3ffn' size='340' side='right'caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ffn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ffn]] 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=3FFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFN FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</div></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]] 3Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">GSN ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [https://pdbe.org/3ffn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [https://www.ebi.ac.uk/pdbsum/3ffn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffn 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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [https://pdbe.org/3ffn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [https://www.ebi.ac.uk/pdbsum/3ffn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffn ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[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>	+	[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 ==
-	[[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>	+	[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]]
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	</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=3ffn 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=3ffn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Gelsolin consists of six homologous domains (G1-G6), each containing a conserved Ca-binding site. Occupation of a subset of these sites enables gelsolin to sever and cap actin filaments in a Ca-dependent manner. Here, we present the structures of Ca-free human gelsolin and of Ca-bound human G1-G3 in a complex with actin. These structures closely resemble those determined previously for equine gelsolin. However, the G2 Ca-binding site is occupied in the human G1-G3/actin structure, whereas it is vacant in the equine version. In-depth comparison of the Ca-free and Ca-activated, actin-bound human gelsolin structures suggests G2 and G6 to be cooperative in binding Ca(2+) and responsible for opening the G2-G6 latch to expose the F-actin-binding site on G2. Mutational analysis of the G2 and G6 Ca-binding sites demonstrates their interdependence in maintaining the compact structure in the absence of calcium. Examination of Ca binding by G2 in human G1-G3/actin reveals that the Ca(2+) locks the G2-G3 interface. Thermal denaturation studies of G2-G3 indicate that Ca binding stabilizes this fragment, driving it into the active conformation. The G2 Ca-binding site is mutated in gelsolin from familial amyloidosis (Finnish-type) patients. This disease initially proceeds through protease cleavage of G2, ultimately to produce a fragment that forms amyloid fibrils. The data presented here support a mechanism whereby the loss of Ca binding by G2 prolongs the lifetime of partially activated, intermediate conformations in which the protease cleavage site is exposed.
-
-	Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.,Nag S, Ma Q, Wang H, Chumnarnsilpa S, Lee WL, Larsson M, Kannan B, Hernandez-Valladares M, Burtnick LD, Robinson RC Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13713-8. Epub 2009 Aug 4. PMID:19666512<ref>PMID:19666512</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3ffn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Burtnick~~, L D~~]]	+	[[Category: Burtnick LD]]
-	[[Category: Chumnarnsilpa, S]]	+	[[Category: Chumnarnsilpa S]]
-	[[Category: Robinson~~, R C]]~~	+	[[Category: Robinson RC]]
-	~~[[Category: Actin]]~~	+
-	~~[[Category: Actin binding protein]]~~	+
-	~~[[Category: Actin capping]]~~	+
-	~~[[Category: Actin-binding]]~~	+
-	~~[[Category: Alternative initiation]]~~	+
-	~~[[Category: Amyloid]]~~	+
-	~~[[Category: Amyloidosis]]~~	+
-	~~[[Category: Ca-dependent]]~~	+
-	~~[[Category: Calcium]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Disulfide bond]]~~	+
-	~~[[Category: Gelsolin]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Secreted~~]]	+

OCA at 08:00, 2 March 2022

OCA — Wed, 02 Mar 2022 08:00:22 GMT

←Older revision		Revision as of 08:00, 2 March 2022
Line 1:		Line 1:

	==Crystal structure of calcium-free human gelsolin==		==Crystal structure of calcium-free human gelsolin==
-	<StructureSection load='3ffn' size='340' side='right' caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='3ffn' size='340' side='right'caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ffn]] 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=3FFN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3FFN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ffn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFN FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([https://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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [~~http~~://pdbe.org/3ffn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ffn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffn 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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [https://pdbe.org/3ffn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [https://www.ebi.ac.uk/pdbsum/3ffn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffn 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]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/3ffn_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/3ffn_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>
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3ffn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ffn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Gelsolin 3D structures\|Gelsolin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Burtnick, L D]]		[[Category: Burtnick, L D]]
	[[Category: Chumnarnsilpa, S]]		[[Category: Chumnarnsilpa, S]]

OCA at 06:40, 1 November 2017

OCA — Wed, 01 Nov 2017 06:40:53 GMT

←Older revision		Revision as of 06:40, 1 November 2017
Line 1:		Line 1:
		+
	==Crystal structure of calcium-free human gelsolin==		==Crystal structure of calcium-free human gelsolin==
	<StructureSection load='3ffn' size='340' side='right' caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3ffn' size='340' side='right' caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [http://pdbe.org/3ffn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [http://www.ebi.ac.uk/pdbsum/3ffn 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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [http://pdbe.org/3ffn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [http://www.ebi.ac.uk/pdbsum/3ffn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffn ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3ffn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ffn" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Gelsolin\|Gelsolin]]
	== References ==		== References ==
	<references/>		<references/>
Line 49:		Line 47:
	[[Category: Amyloidosis]]		[[Category: Amyloidosis]]
	[[Category: Ca-dependent]]		[[Category: Ca-dependent]]
		+	[[Category: Calcium]]
		+	[[Category: Cytoplasm]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
Line 54:		Line 54:
	[[Category: Gelsolin]]		[[Category: Gelsolin]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
		+	[[Category: Polymorphism]]
	[[Category: Secreted]]		[[Category: Secreted]]

OCA at 00:25, 9 February 2016

OCA — Tue, 09 Feb 2016 00:25:50 GMT

←Older revision		Revision as of 00:25, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='3ffn' size='340' side='right' caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3ffn' size='340' side='right' caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ffn]] is a 2 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=3FFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ffn]] 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=3FFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFN FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [http://www.ebi.ac.uk/pdbsum/3ffn 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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [http://pdbe.org/3ffn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [http://www.ebi.ac.uk/pdbsum/3ffn PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 19:
	<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=3ffn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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 3ffn" 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: Chumnarnsilpa, S]]		[[Category: Chumnarnsilpa, S]]

OCA at 13:11, 18 December 2014

OCA — Thu, 18 Dec 2014 13:11:44 GMT

←Older revision		Revision as of 13:11, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3ffn~~\| ~~PDB~~=3ffn \| ~~SCENE~~= }}	+	==Crystal structure of calcium-free human gelsolin==
-	===~~Crystal~~ structure of ~~calcium~~-~~free human gelsolin~~===	+	<StructureSection load='3ffn' size='340' side='right' caption='[[3ffn]], [[Resolution\|resolution]] 3.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19666512}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ffn]] is a 2 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=3FFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFN FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1d0n\|1d0n]], [[1h1v\|1h1v]], [[1p8x\|1p8x]], [[1p8z\|1p8z]], [[1rgi\|1rgi]], [[2fgh\|2fgh]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3ffn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffn RCSB], [http://www.ebi.ac.uk/pdbsum/3ffn 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/ff/3ffn_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 consists of six homologous domains (G1-G6), each containing a conserved Ca-binding site. Occupation of a subset of these sites enables gelsolin to sever and cap actin filaments in a Ca-dependent manner. Here, we present the structures of Ca-free human gelsolin and of Ca-bound human G1-G3 in a complex with actin. These structures closely resemble those determined previously for equine gelsolin. However, the G2 Ca-binding site is occupied in the human G1-G3/actin structure, whereas it is vacant in the equine version. In-depth comparison of the Ca-free and Ca-activated, actin-bound human gelsolin structures suggests G2 and G6 to be cooperative in binding Ca(2+) and responsible for opening the G2-G6 latch to expose the F-actin-binding site on G2. Mutational analysis of the G2 and G6 Ca-binding sites demonstrates their interdependence in maintaining the compact structure in the absence of calcium. Examination of Ca binding by G2 in human G1-G3/actin reveals that the Ca(2+) locks the G2-G3 interface. Thermal denaturation studies of G2-G3 indicate that Ca binding stabilizes this fragment, driving it into the active conformation. The G2 Ca-binding site is mutated in gelsolin from familial amyloidosis (Finnish-type) patients. This disease initially proceeds through protease cleavage of G2, ultimately to produce a fragment that forms amyloid fibrils. The data presented here support a mechanism whereby the loss of Ca binding by G2 prolongs the lifetime of partially activated, intermediate conformations in which the protease cleavage site is exposed.

-	~~==Disease==~~	+	Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.,Nag S, Ma Q, Wang H, Chumnarnsilpa S, Lee WL, Larsson M, Kannan B, Hernandez-Valladares M, Burtnick LD, Robinson RC Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13713-8. Epub 2009 Aug 4. PMID:19666512<ref>PMID:19666512</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==~~	+
-	[[3ffn]] is a 2 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=3FFN OCA].	+

	==See Also==		==See Also==
	*[[Gelsolin\|Gelsolin]]		*[[Gelsolin\|Gelsolin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019666512</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Burtnick, L D.]]	+	[[Category: Burtnick, L D]]
-	[[Category: Chumnarnsilpa, S.]]	+	[[Category: Chumnarnsilpa, S]]
-	[[Category: Robinson, R C.]]	+	[[Category: Robinson, R C]]
	[[Category: Actin]]		[[Category: Actin]]
	[[Category: Actin binding protein]]		[[Category: Actin binding protein]]

OCA at 23:45, 24 March 2013

OCA — Sun, 24 Mar 2013 23:45:41 GMT

←Older revision		Revision as of 23:45, 24 March 2013
Line 1:		Line 1:
-	[[Image:3ffn.png\|left\|200px]]
-
	{{STRUCTURE_3ffn\| PDB=3ffn \| SCENE= }}		{{STRUCTURE_3ffn\| PDB=3ffn \| SCENE= }}
-
	===Crystal structure of calcium-free human gelsolin===		===Crystal structure of calcium-free human gelsolin===
		+	{{ABSTRACT_PUBMED_19666512}}

-	~~{{ABSTRACT_PUBMED_19666512}}~~	+	==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:019666512</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019666512</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]

OCA at 11:59, 20 October 2012

OCA — Sat, 20 Oct 2012 11:59:43 GMT

←Older revision		Revision as of 11:59, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3ffn]] is a 2 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=3FFN OCA].	+	[[3ffn]] is a 2 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=3FFN OCA].

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

OCA at 07:16, 26 July 2012

OCA — Thu, 26 Jul 2012 07:16:42 GMT

←Older revision		Revision as of 07:16, 26 July 2012
Line 1:		Line 1:
	[[Image:3ffn.png\|left\|200px]]		[[Image:3ffn.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ffn", 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_3ffn\| PDB=3ffn \| SCENE= }}		{{STRUCTURE_3ffn\| PDB=3ffn \| SCENE= }}

	===Crystal structure of calcium-free human gelsolin===		===Crystal structure of calcium-free human gelsolin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19666512}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19666512 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19666512}}		{{ABSTRACT_PUBMED_19666512}}

Line 22:		Line 11:

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19666512~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019666512</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Burtnick, L D.]]		[[Category: Burtnick, L D.]]
Line 38:		Line 27:
	[[Category: Amyloidosis]]		[[Category: Amyloidosis]]
	[[Category: Ca-dependent]]		[[Category: Ca-dependent]]
-	[[Category: Calcium]]
-	[[Category: Cytoplasm]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
Line 45:		Line 32:
	[[Category: Gelsolin]]		[[Category: Gelsolin]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
	[[Category: Secreted]]		[[Category: Secreted]]

OCA: Protected "3ffn" [edit=sysop:move=sysop]

OCA — Sun, 26 Dec 2010 09:37:44 GMT

Protected "3ffn" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:37, 26 December 2010

OCA at 09:37, 26 December 2010

OCA — Sun, 26 Dec 2010 09:37:43 GMT

←Older revision		Revision as of 09:37, 26 December 2010
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3ffn.png\|left\|200px]]
-	[[Image:3ffn.~~jpg~~\|left\|200px]]	+

	<!--		<!--
Line 18:		Line 17:
	-->		-->
	{{ABSTRACT_PUBMED_19666512}}		{{ABSTRACT_PUBMED_19666512}}
-
-	==Disease==
-	Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=137350 137350]]

	==About this Structure==		==About this Structure==
-	~~3FFN~~ is a 2 ~~chains~~ structure of ~~sequences~~ 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=3FFN OCA].	+	[[3ffn]] is a 2 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=3FFN OCA].
		+
		+	==See Also==
		+	*[[Gelsolin]]

	==Reference==		==Reference==
Line 48:		Line 47:
	[[Category: Polymorphism]]		[[Category: Polymorphism]]
	[[Category: Secreted]]		[[Category: Secreted]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 7 13:53:52 2009''