1q8x - Revision history

OCA at 09:01, 22 May 2024

OCA — Wed, 22 May 2024 09:01:35 GMT

←Older revision		Revision as of 09:01, 22 May 2024
Line 19:		Line 19:
	</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=1q8x 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=1q8x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human actin-depolymerizing factor (ADF) and cofilin are pH-sensitive, actin-depolymerizing proteins. Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8. To understand this, we solved the structure of human cofilin using nuclear magnetic resonance and compared it with human ADF. Important sequence differences between vertebrate ADF/cofilins were correlated with unique structural determinants in the F-actin-binding site to account for differences in biochemical activities of the two proteins. Cofilin has a short beta-strand at the C terminus, not found in ADF, which packs against strands beta3/beta4, changing the environment around Lys96, a residue essential for F-actin binding. A salt bridge involving His133 and Asp98 (Glu98 in ADF) may explain the pH sensitivity of human cofilin and ADF; these two residues are fully conserved in vertebrate ADF/cofilins. Chemical shift perturbations identified residues that (i) differ in their chemical environments between wild type cofilin and mutants S3D, which has greatly reduced G-actin binding, and K96Q, which does not bind F-actin; (ii) are affected when G-actin binds cofilin; and (iii) are affected by pH change from 6 to 8. Many residues affected by G-actin binding also show perturbation in the mutants or in response to pH. Our evidence suggests the involvement of residues 133-138 of strand beta5 in all of the activities examined. Because residues in beta5 are perturbed by mutations that affect both G-actin and F-actin binding, this strand forms a "boundary" or "bridge" between the proposed F- and G-actin-binding sites.
		+
		+	Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor.,Pope BJ, Zierler-Gould KM, Kuhne R, Weeds AG, Ball LJ J Biol Chem. 2004 Feb 6;279(6):4840-8. Epub 2003 Nov 18. PMID:14627701<ref>PMID:14627701</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:02, 17 April 2024

OCA — Wed, 17 Apr 2024 06:02:30 GMT

←Older revision		Revision as of 06:02, 17 April 2024
Line 1:		Line 1:

	==NMR structure of human cofilin==		==NMR structure of human cofilin==
-	<StructureSection load='1q8x' size='340' side='right'caption='[[1q8x~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1q8x' size='340' side='right'caption='[[1q8x]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q8X 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;'>[[1q8g\|1q8g]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [https://pdbe.org/1q8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [https://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x 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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [https://pdbe.org/1q8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [https://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN]] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref>	+	[https://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 19:
	</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=1q8x 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=1q8x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human actin-depolymerizing factor (ADF) and cofilin are pH-sensitive, actin-depolymerizing proteins. Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8. To understand this, we solved the structure of human cofilin using nuclear magnetic resonance and compared it with human ADF. Important sequence differences between vertebrate ADF/cofilins were correlated with unique structural determinants in the F-actin-binding site to account for differences in biochemical activities of the two proteins. Cofilin has a short beta-strand at the C terminus, not found in ADF, which packs against strands beta3/beta4, changing the environment around Lys96, a residue essential for F-actin binding. A salt bridge involving His133 and Asp98 (Glu98 in ADF) may explain the pH sensitivity of human cofilin and ADF; these two residues are fully conserved in vertebrate ADF/cofilins. Chemical shift perturbations identified residues that (i) differ in their chemical environments between wild type cofilin and mutants S3D, which has greatly reduced G-actin binding, and K96Q, which does not bind F-actin; (ii) are affected when G-actin binds cofilin; and (iii) are affected by pH change from 6 to 8. Many residues affected by G-actin binding also show perturbation in the mutants or in response to pH. Our evidence suggests the involvement of residues 133-138 of strand beta5 in all of the activities examined. Because residues in beta5 are perturbed by mutations that affect both G-actin and F-actin binding, this strand forms a "boundary" or "bridge" between the proposed F- and G-actin-binding sites.
-
-	Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor.,Pope BJ, Zierler-Gould KM, Kuhne R, Weeds AG, Ball LJ J Biol Chem. 2004 Feb 6;279(6):4840-8. Epub 2003 Nov 18. PMID:14627701<ref>PMID:14627701</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ball~~, L J~~]]	+	[[Category: Ball LJ]]
-	[[Category: Kuhne, R]]	+	[[Category: Kuhne R]]
-	[[Category: Pope~~, B J~~]]	+	[[Category: Pope BJ]]
-	[[Category: Weeds~~, A G~~]]	+	[[Category: Weeds AG]]
-	[[Category: Zierler-Gould~~, K M]]~~	+	[[Category: Zierler-Gould KM]]
-	~~[[Category: Actin cytoskeleton]]~~	+
-	~~[[Category: Adf/cofilin]]~~	+
-	~~[[Category: Chemical shift perturbation]]~~	+
-	~~[[Category: G-actin binding]]~~	+
-	~~[[Category: Structural protein~~]]	+

OCA at 06:26, 2 March 2022

OCA — Wed, 02 Mar 2022 06:26:57 GMT

←Older revision		Revision as of 06:26, 2 March 2022
Line 3:		Line 3:
	<StructureSection load='1q8x' size='340' side='right'caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1q8x' size='340' side='right'caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q8X 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;'>[[1q8g\|1q8g]]</div></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;'>[[1q8g\|1q8g]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([~~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">CFL1 OR CFL ([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~~://proteopedia.org/fgij/fg.htm?mol=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [~~http~~://pdbe.org/1q8x PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x 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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [https://pdbe.org/1q8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [https://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN]] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref>	+	[[https://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN]] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Eukaryotic initiation factor 3D structures\|Eukaryotic initiation factor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:46, 9 December 2020

OCA — Wed, 09 Dec 2020 07:46:03 GMT

←Older revision		Revision as of 07:46, 9 December 2020
Line 1:		Line 1:

	==NMR structure of human cofilin==		==NMR structure of human cofilin==
-	<StructureSection load='1q8x' size='340' side='right' caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1q8x' size='340' side='right'caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</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;'>[[1q8g\|1q8g]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([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">CFL1 OR CFL ([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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://pdbe.org/1q8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://pdbe.org/1q8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Eukaryotic initiation factor 3D structures\|Eukaryotic initiation factor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ball, L J]]		[[Category: Ball, L J]]
	[[Category: Kuhne, R]]		[[Category: Kuhne, R]]

OCA at 08:34, 24 February 2018

OCA — Sat, 24 Feb 2018 08:34:24 GMT

←Older revision		Revision as of 08:34, 24 February 2018
Line 1:		Line 1:
		+
	==NMR structure of human cofilin==		==NMR structure of human cofilin==
	<StructureSection load='1q8x' size='340' side='right' caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1q8x' size='340' side='right' caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([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">CFL1 OR CFL ([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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://pdbe.org/1q8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x 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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://pdbe.org/1q8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q8/1q8x_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q8/1q8x_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=1q8x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1q8x" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Eukaryotic initiation factor\|Eukaryotic initiation factor]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 01:11, 12 September 2015

OCA — Sat, 12 Sep 2015 01:11:08 GMT

←Older revision		Revision as of 01:11, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='1q8x' size='340' side='right' caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1q8x' size='340' side='right' caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([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">CFL1 OR CFL ([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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x 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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://pdbe.org/1q8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1q8x" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ball, L J]]		[[Category: Ball, L J]]
	[[Category: Kuhne, R]]		[[Category: Kuhne, R]]

OCA at 21:50, 25 December 2014

OCA — Thu, 25 Dec 2014 21:50:20 GMT

←Older revision		Revision as of 21:50, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([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">CFL1 OR CFL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x 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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN]] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Ball, L J.]]	+	[[Category: Ball, L J]]
-	[[Category: Kuhne, R.]]	+	[[Category: Kuhne, R]]
-	[[Category: Pope, B J.]]	+	[[Category: Pope, B J]]
-	[[Category: Weeds, A G.]]	+	[[Category: Weeds, A G]]
-	[[Category: Zierler-Gould, K M.]]	+	[[Category: Zierler-Gould, K M]]
	[[Category: Actin cytoskeleton]]		[[Category: Actin cytoskeleton]]
	[[Category: Adf/cofilin]]		[[Category: Adf/cofilin]]

OCA at 23:08, 28 September 2014

OCA — Sun, 28 Sep 2014 23:08:02 GMT

←Older revision		Revision as of 23:08, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1q8x.~~png~~\|~~left~~\|200px]]	+	==NMR structure of human cofilin==
		+	<StructureSection load='1q8x' size='340' side='right' caption='[[1q8x]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q8X FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1q8g\|1q8g]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1 OR CFL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1q8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q8x RCSB], [http://www.ebi.ac.uk/pdbsum/1q8x PDBsum]</span></td></tr>
		+	<table>
		+	== 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/q8/1q8x_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 ==
		+	Human actin-depolymerizing factor (ADF) and cofilin are pH-sensitive, actin-depolymerizing proteins. Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8. To understand this, we solved the structure of human cofilin using nuclear magnetic resonance and compared it with human ADF. Important sequence differences between vertebrate ADF/cofilins were correlated with unique structural determinants in the F-actin-binding site to account for differences in biochemical activities of the two proteins. Cofilin has a short beta-strand at the C terminus, not found in ADF, which packs against strands beta3/beta4, changing the environment around Lys96, a residue essential for F-actin binding. A salt bridge involving His133 and Asp98 (Glu98 in ADF) may explain the pH sensitivity of human cofilin and ADF; these two residues are fully conserved in vertebrate ADF/cofilins. Chemical shift perturbations identified residues that (i) differ in their chemical environments between wild type cofilin and mutants S3D, which has greatly reduced G-actin binding, and K96Q, which does not bind F-actin; (ii) are affected when G-actin binds cofilin; and (iii) are affected by pH change from 6 to 8. Many residues affected by G-actin binding also show perturbation in the mutants or in response to pH. Our evidence suggests the involvement of residues 133-138 of strand beta5 in all of the activities examined. Because residues in beta5 are perturbed by mutations that affect both G-actin and F-actin binding, this strand forms a "boundary" or "bridge" between the proposed F- and G-actin-binding sites.

-	~~{{STRUCTURE_1q8x\| PDB=1q8x \| SCENE= }}~~	+	Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor.,Pope BJ, Zierler-Gould KM, Kuhne R, Weeds AG, Ball LJ J Biol Chem. 2004 Feb 6;279(6):4840-8. Epub 2003 Nov 18. PMID:14627701<ref>PMID:14627701</ref>

-	~~===NMR structure~~ of ~~human cofilin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14627701}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1q8x]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA].~~	+

	==See Also==		==See Also==
	*[[Eukaryotic initiation factor\|Eukaryotic initiation factor]]		*[[Eukaryotic initiation factor\|Eukaryotic initiation factor]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:014627701<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ball, L J.]]		[[Category: Ball, L J.]]

OCA: Protected "1q8x" [edit=sysop:move=sysop]

OCA — Sat, 20 Oct 2012 22:03:56 GMT

Protected "1q8x" [edit=sysop:move=sysop]

←Older revision

Revision as of 22:03, 20 October 2012

OCA at 22:03, 20 October 2012

OCA — Sat, 20 Oct 2012 22:03:53 GMT

←Older revision		Revision as of 22:03, 20 October 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1q8x.png\|left\|200px]]		[[Image:1q8x.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1q8x", 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_1q8x\| PDB=1q8x \| SCENE= }}		{{STRUCTURE_1q8x\| PDB=1q8x \| SCENE= }}

	===NMR structure of human cofilin===		===NMR structure of human cofilin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14627701}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14627701 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14627701}}		{{ABSTRACT_PUBMED_14627701}}

	==About this Structure==		==About this Structure==
-	~~1Q8X~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA].	+	[[1q8x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8X OCA].
		+
		+	==See Also==
		+	*[[Eukaryotic initiation factor\|Eukaryotic initiation factor]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14627701~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014627701</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ball, L J.]]		[[Category: Ball, L J.]]
Line 34:		Line 25:
	[[Category: Chemical shift perturbation]]		[[Category: Chemical shift perturbation]]
	[[Category: G-actin binding]]		[[Category: G-actin binding]]
-	[[Category: ~~Nmr~~]]	+	[[Category: Structural protein]]
-		+
-	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:56:35 2009''~~	+