4eah - Revision history

OCA at 11:02, 1 March 2024

2024-03-01T11:02:49Z

← Older revision		Revision as of 11:02, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.4Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [https://pdbe.org/4eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [https://www.ebi.ac.uk/pdbsum/4eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah 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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [https://pdbe.org/4eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [https://www.ebi.ac.uk/pdbsum/4eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[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.		[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 ==~~
	Formins are actin-assembly factors that act in a variety of actin-based processes. The conserved formin homology 2 (FH2) domain promotes filament nucleation and influences elongation through interaction with the barbed end. FMNL3 is a formin that induces assembly of filopodia but whose FH2 domain is a poor nucleator. The 3.4-A structure of a mouse FMNL3 FH2 dimer in complex with tetramethylrhodamine-actin uncovers details of formin-regulated actin elongation. We observe distinct FH2 actin-binding regions; interactions in the knob and coiled-coil subdomains are necessary for actin binding, whereas those in the lasso-post interface are important for the stepping mechanism. Biochemical and cellular experiments test the importance of individual residues for function. This structure provides details for FH2-mediated filament elongation by processive capping and supports a model in which C-terminal non-FH2 residues of FMNL3 are required to stabilize the filament nucleus.

	FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.,Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ Nat Struct Mol Biol. 2012 Dec 9. doi: 10.1038/nsmb.2462. PMID:23222643<ref>PMID:23222643</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Actin 3D structures\|Actin 3D structures]]		*[[Actin 3D structures\|Actin 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:00, 28 September 2022

2022-09-28T07:00:10Z

← Older revision		Revision as of 07:00, 28 September 2022
Line 1:		Line 1:

	==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==		==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==
	<StructureSection load='4eah' size='340' side='right' caption='[[4eah]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='4eah' size='340' side='right'caption='[[4eah]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EAH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fmnl3, Kiaa2014 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [https://pdbe.org/4eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [https://www.ebi.ac.uk/pdbsum/4eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah 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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [~~http~~://pdbe.org/4eah PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4eah PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah 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/FMNL3_MOUSE FMNL3_MOUSE]] Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity).		[[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Actin 3D structures\|Actin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Large Structures]]
			[[Category: Mus musculus]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Gauvin~~, T J~~]]		[[Category: Gauvin TJ]]
	[[Category: Heimsath~~, E G~~]]		[[Category: Heimsath EG]]
	[[Category: Higgs~~, H N~~]]		[[Category: Higgs HN]]
	[[Category: Kull~~, F J~~]]		[[Category: Kull FJ]]
	[[Category: Thompson~~, M E]]~~		[[Category: Thompson ME]]
	~~[[Category: Actin]]~~
	~~[[Category: Atp binding]]~~
	~~[[Category: Cytoskeleton]]~~
	~~[[Category: Fmnl3]]~~
	~~[[Category: Formin]]~~
	~~[[Category: Protein binding~~]]

OCA at 08:00, 15 November 2017

2017-11-15T08:00:53Z

← Older revision		Revision as of 08:00, 15 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4eah" style="background-color:#fffaf0;"></div>

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

OCA at 13:55, 4 August 2016

2016-08-04T13:55:39Z

← Older revision		Revision as of 13:55, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==		==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==
	<StructureSection load='4eah' size='340' side='right' caption='[[4eah]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='4eah' size='340' side='right' caption='[[4eah]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EAH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fmnl3, Kiaa2014 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fmnl3, Kiaa2014 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [http://www.ebi.ac.uk/pdbsum/4eah 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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [http://pdbe.org/4eah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [http://www.ebi.ac.uk/pdbsum/4eah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4eah" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Mus musculus~~]]		[[Category: Lk3 transgenic mice]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Gauvin, T J]]		[[Category: Gauvin, T J]]

OCA at 09:55, 25 December 2014

2014-12-25T09:55:12Z

← Older revision		Revision as of 09:55, 25 December 2014
Line 7:		Line 7:
	<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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [http://www.ebi.ac.uk/pdbsum/4eah 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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [http://www.ebi.ac.uk/pdbsum/4eah PDBsum]</span></td></tr>
	</table>		</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/FMNL3_MOUSE FMNL3_MOUSE]] Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:09, 9 December 2014

2014-12-09T17:09:28Z

← Older revision		Revision as of 17:09, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4eah~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==
			<StructureSection load='4eah' size='340' side='right' caption='[[4eah]], [[Resolution\|resolution]] 3.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Fmnl3, Kiaa2014 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [http://www.ebi.ac.uk/pdbsum/4eah PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Formins are actin-assembly factors that act in a variety of actin-based processes. The conserved formin homology 2 (FH2) domain promotes filament nucleation and influences elongation through interaction with the barbed end. FMNL3 is a formin that induces assembly of filopodia but whose FH2 domain is a poor nucleator. The 3.4-A structure of a mouse FMNL3 FH2 dimer in complex with tetramethylrhodamine-actin uncovers details of formin-regulated actin elongation. We observe distinct FH2 actin-binding regions; interactions in the knob and coiled-coil subdomains are necessary for actin binding, whereas those in the lasso-post interface are important for the stepping mechanism. Biochemical and cellular experiments test the importance of individual residues for function. This structure provides details for FH2-mediated filament elongation by processive capping and supports a model in which C-terminal non-FH2 residues of FMNL3 are required to stabilize the filament nucleus.

	~~{{STRUCTURE_4eah\| PDB=4eah \| SCENE= }}~~		FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.,Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ Nat Struct Mol Biol. 2012 Dec 9. doi: 10.1038/nsmb.2462. PMID:23222643<ref>PMID:23222643</ref>

	~~===Crystal structure~~ of the ~~formin homology 2 domain of FMNL3 bound to actin===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_23222643}}~~

	~~==About this Structure==~~
	~~[[4eah]] is a 8 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA].~~

	==See Also==		==See Also==
	*[[Actin\|Actin]]		*[[Actin\|Actin]]
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Gauvin, T J.]]		[[Category: Gauvin, T J]]
	[[Category: Heimsath, E G.]]		[[Category: Heimsath, E G]]
	[[Category: Higgs, H N.]]		[[Category: Higgs, H N]]
	[[Category: Kull, F J.]]		[[Category: Kull, F J]]
	[[Category: Thompson, M E.]]		[[Category: Thompson, M E]]
	[[Category: Actin]]		[[Category: Actin]]
	[[Category: Atp binding]]		[[Category: Atp binding]]

OCA at 10:35, 23 January 2013

2013-01-23T10:35:44Z

← Older revision		Revision as of 10:35, 23 January 2013
Line 9:		Line 9:
	==About this Structure==		==About this Structure==
	[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA].		[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA].

			==See Also==
			*[[Actin\|Actin]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]

OCA at 06:57, 2 January 2013

2013-01-02T06:57:38Z

← Older revision		Revision as of 06:57, 2 January 2013
Line 1:		Line 1:
	[[Image:4eah.~~jpg~~\|left\|200px]]		[[Image:4eah.png\|left\|200px]]

	{{STRUCTURE_4eah\| PDB=4eah \| SCENE= }}		{{STRUCTURE_4eah\| PDB=4eah \| SCENE= }}
Line 5:		Line 5:
	===Crystal structure of the formin homology 2 domain of FMNL3 bound to actin===		===Crystal structure of the formin homology 2 domain of FMNL3 bound to actin===

			{{ABSTRACT_PUBMED_23222643}}

	==About this Structure==		==About this Structure==

OCA at 21:25, 12 December 2012

2012-12-12T21:25:22Z

← Older revision		Revision as of 21:25, 12 December 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4eah.jpg\|left\|200px]]

	~~The entry~~ 4eah ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4eah\| PDB=4eah \| SCENE= }}

	~~Authors: Thompson, M.E., Heimsath, E.G., Gauvin, T.J., Higgs, H.N., Kull, F.J.~~		===Crystal structure of the formin homology 2 domain of FMNL3 bound to actin===

	~~Description~~: ~~Crystal structure of the formin homology 2 domain of FMNL3 bound to actin~~
			==About this Structure==
			[[4eah]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=4EAH OCA].
			[[Category: Mus musculus]]
			[[Category: Oryctolagus cuniculus]]
			[[Category: Gauvin, T J.]]
			[[Category: Heimsath, E G.]]
			[[Category: Higgs, H N.]]
			[[Category: Kull, F J.]]
			[[Category: Thompson, M E.]]
			[[Category: Actin]]
			[[Category: Atp binding]]
			[[Category: Cytoskeleton]]
			[[Category: Fmnl3]]
			[[Category: Formin]]
			[[Category: Protein binding]]

OCA at 07:11, 4 July 2012

2012-07-04T07:11:49Z

← Older revision		Revision as of 07:11, 4 July 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Thompson, M.E., Heimsath, E.G., Gauvin, T.J., Higgs, H.N., Kull, F.J.		Authors: Thompson, M.E., Heimsath, E.G., Gauvin, T.J., Higgs, H.N., Kull, F.J.

	Description: Crystal structure of the formin homology 2 domain of FMNL3 bound to actin		Description: Crystal structure of the formin homology 2 domain of FMNL3 bound to actin