4eah: Difference between revisions
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[[ | ==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. | |||
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> | |||
==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]] | ||
Revision as of 20:09, 9 December 2014
Crystal structure of the formin homology 2 domain of FMNL3 bound to actinCrystal structure of the formin homology 2 domain of FMNL3 bound to actin
Structural highlights
Publication Abstract from PubMedFormins 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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