6vao - Revision history

OCA at 14:36, 6 March 2024

OCA — Wed, 06 Mar 2024 14:36:54 GMT

←Older revision		Revision as of 14:36, 6 March 2024
Line 3:		Line 3:
	<SX load='6vao' size='340' side='right' viewer='molstar' caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>		<SX load='6vao' size='340' side='right' viewer='molstar' caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~] and [~~http~~://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6VAO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VAO FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.4Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[6uby\|6uby]], [[6uc4\|6uc4]], [[6uc0\|6uc0]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<~~tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">CFL1, 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'>[https://proteopedia.org/fgij/fg.htm?mol=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [https://pdbe.org/6vao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [https://www.ebi.ac.uk/pdbsum/6vao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao 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=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [~~http~~://pdbe.org/6vao PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6vao PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/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/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with positive cooperativity, forming clusters of contiguously bound cofilin along the filament lattice. Filament severing occurs preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments and is biased at 1 side of a cluster. A molecular understanding of cooperative binding and filament severing has been impeded by a lack of structural data describing boundaries. Here, we apply methods for analyzing filament cryo-electron microscopy (cryo-EM) data at the single subunit level to directly investigate the structure of boundaries within partially decorated cofilactin filaments. Subnanometer resolution maps of isolated, bound cofilin molecules and an actin-cofilactin boundary indicate that cofilin-induced actin conformational changes are local and limited to subunits directly contacting bound cofilin. An isolated, bound cofilin compromises longitudinal filament contacts of 1 protofilament, consistent with a single cofilin having filament-severing activity. An individual, bound phosphomimetic (S3D) cofilin with weak severing activity adopts a unique binding mode that does not perturb actin structure. Cofilin clusters disrupt both protofilaments, consistent with a higher severing activity at boundaries compared to single cofilin. Comparison of these structures indicates that this disruption is substantially greater at pointed end sides of cofilactin clusters than at the barbed end. These structures, with the distribution of bound cofilin clusters, suggest that maximum binding cooperativity is achieved when 2 cofilins occupy adjacent sites. These results reveal the structural origins of cooperative cofilin binding and actin filament severing.	+

-	Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.,Huehn AR, Bibeau JP, Schramm AC, Cao W, De La Cruz EM, Sindelar CV Proc Natl Acad Sci U S A. 2020 Jan 21;117(3):1478-1484. doi:, 10.1073/pnas.1915987117. Epub 2020 Jan 3. PMID:31900364<ref>PMID:31900364</ref>	+	==See Also==
-		+	*[[Actin 3D structures\|Actin 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6vao" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	[[Category: Bibeau~~, J P~~]]	+	[[Category: Bibeau JP]]
-	[[Category: Cao, W]]	+	[[Category: Cao W]]
-	[[Category: ~~Cruz, E M.~~De La]]	+	[[Category: De La Cruz EM]]
-	[[Category: Huehn~~, A R~~]]	+	[[Category: Huehn AR]]
-	[[Category: Schramm~~, A C~~]]	+	[[Category: Schramm AC]]
-	[[Category: Sindelar~~, C V]]~~	+	[[Category: Sindelar CV]]
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Structural protein~~]]	+

OCA at 07:06, 11 April 2020

OCA — Sat, 11 Apr 2020 07:06:55 GMT

←Older revision		Revision as of 07:06, 11 April 2020
Line 3:		Line 3:
	<SX load='6vao' size='340' side='right' viewer='molstar' caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>		<SX load='6vao' size='340' side='right' viewer='molstar' caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6VAO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VAO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6uby\|6uby]], [[6uc4\|6uc4]], [[6uc0\|6uc0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6uby\|6uby]], [[6uc4\|6uc4]], [[6uc0\|6uc0]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1, 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, 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=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [http://pdbe.org/6vao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [http://www.ebi.ac.uk/pdbsum/6vao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao 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=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [http://pdbe.org/6vao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [http://www.ebi.ac.uk/pdbsum/6vao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 01:24, 7 March 2020

OCA — Sat, 07 Mar 2020 01:24:57 GMT

←Older revision		Revision as of 01:24, 7 March 2020
Line 1:		Line 1:

	==Human cofilin-1 decorated actin filament==		==Human cofilin-1 decorated actin filament==
-	<~~StructureSection~~ load='6vao' size='340' side='right'caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>	+	<SX load='6vao' size='340' side='right' viewer='molstar' caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAO FirstGlance]. <br>		<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAO FirstGlance]. <br>
Line 23:		Line 23:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Human]]		[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 09:11, 5 February 2020

OCA — Wed, 05 Feb 2020 09:11:08 GMT

←Older revision		Revision as of 09:11, 5 February 2020
Line 3:		Line 3:
	<StructureSection load='6vao' size='340' side='right'caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='6vao' size='340' side='right'caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6uby\|6uby]], [[6uc4\|6uc4]], [[6uc0\|6uc0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6uby\|6uby]], [[6uc4\|6uc4]], [[6uc0\|6uc0]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFL1, 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=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [http://pdbe.org/6vao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [http://www.ebi.ac.uk/pdbsum/6vao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [http://pdbe.org/6vao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [http://www.ebi.ac.uk/pdbsum/6vao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/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>		[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with positive cooperativity, forming clusters of contiguously bound cofilin along the filament lattice. Filament severing occurs preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments and is biased at 1 side of a cluster. A molecular understanding of cooperative binding and filament severing has been impeded by a lack of structural data describing boundaries. Here, we apply methods for analyzing filament cryo-electron microscopy (cryo-EM) data at the single subunit level to directly investigate the structure of boundaries within partially decorated cofilactin filaments. Subnanometer resolution maps of isolated, bound cofilin molecules and an actin-cofilactin boundary indicate that cofilin-induced actin conformational changes are local and limited to subunits directly contacting bound cofilin. An isolated, bound cofilin compromises longitudinal filament contacts of 1 protofilament, consistent with a single cofilin having filament-severing activity. An individual, bound phosphomimetic (S3D) cofilin with weak severing activity adopts a unique binding mode that does not perturb actin structure. Cofilin clusters disrupt both protofilaments, consistent with a higher severing activity at boundaries compared to single cofilin. Comparison of these structures indicates that this disruption is substantially greater at pointed end sides of cofilactin clusters than at the barbed end. These structures, with the distribution of bound cofilin clusters, suggest that maximum binding cooperativity is achieved when 2 cofilins occupy adjacent sites. These results reveal the structural origins of cooperative cofilin binding and actin filament severing.
		+
		+	Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.,Huehn AR, Bibeau JP, Schramm AC, Cao W, De La Cruz EM, Sindelar CV Proc Natl Acad Sci U S A. 2020 Jan 21;117(3):1478-1484. doi:, 10.1073/pnas.1915987117. Epub 2020 Jan 3. PMID:31900364<ref>PMID:31900364</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6vao" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]

OCA at 07:42, 8 January 2020

OCA — Wed, 08 Jan 2020 07:42:53 GMT

←Older revision		Revision as of 07:42, 8 January 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6vao ~~is ON HOLD~~	+	==Human cofilin-1 decorated actin filament==
-		+	<StructureSection load='6vao' size='340' side='right'caption='[[6vao]], [[Resolution\|resolution]] 3.40Å' scene=''>
-	~~Authors~~: ~~Huehn, A~~.R., ~~Bibeau~~, J.P., ~~Schramm, A~~.C., ~~Cao~~, W.~~, De La Cruz, E~~.M., ~~Sindelar~~, C.V.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6vao]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAO FirstGlance]. <br>
-	~~Description~~: ~~Human cofilin~~-~~1 decorated~~ actin ~~filament~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6uby\|6uby]], [[6uc4\|6uc4]], [[6uc0\|6uc0]]</td></tr>
-	[[Category: ~~Schramm~~, ~~A.C~~]]	+	<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=6vao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vao OCA], [http://pdbe.org/6vao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vao RCSB], [http://www.ebi.ac.uk/pdbsum/6vao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vao ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Oryctolagus cuniculus]]
		+	[[Category: Bibeau, J P]]
	[[Category: Cao, W]]		[[Category: Cao, W]]
-	[[Category: ~~Sindelar~~, C.V]]	+	[[Category: Cruz, E M.De La]]
-	[[Category: ~~De La Cruz~~, ~~E.M~~]]	+	[[Category: Huehn, A R]]
-	[[Category: ~~Huehn~~, A.R]]	+	[[Category: Schramm, A C]]
-	[[Category: ~~Bibeau~~, ~~J.P~~]]	+	[[Category: Sindelar, C V]]
		+	[[Category: Cytoskeleton]]
		+	[[Category: Structural protein]]

OCA: Protected "6vao" [edit=sysop:move=sysop]

OCA — Wed, 25 Dec 2019 07:36:33 GMT

Protected "6vao" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:36, 25 December 2019

OCA: New page: '''Unreleased structure''' The entry 6vao is ON HOLD Authors: Huehn, A.R., Bibeau, J.P., Schramm, A.C., Cao, W., De La Cruz, E.M., Sindelar, C.V. Description: Human cofilin-1 decorated...

OCA — Wed, 25 Dec 2019 07:36:31 GMT

New page: '''Unreleased structure''' The entry 6vao is ON HOLD Authors: Huehn, A.R., Bibeau, J.P., Schramm, A.C., Cao, W., De La Cruz, E.M., Sindelar, C.V. Description: Human cofilin-1 decorated...

New page

'''Unreleased structure'''

The entry 6vao is ON HOLD

Authors: Huehn, A.R., Bibeau, J.P., Schramm, A.C., Cao, W., De La Cruz, E.M., Sindelar, C.V.

Description: Human cofilin-1 decorated actin filament
[[Category: Unreleased Structures]]
[[Category: Schramm, A.C]]
[[Category: Cao, W]]
[[Category: Sindelar, C.V]]
[[Category: De La Cruz, E.M]]
[[Category: Huehn, A.R]]
[[Category: Bibeau, J.P]]