3daw

From Proteopedia

(Difference between revisions)

Revision as of 12:10, 25 December 2014

Structure of the actin-depolymerizing factor homology domain in complex with actin

Structural highlights

3daw is a 2 chain structure with sequence from Mus musculus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2a42, 2hd7
Gene:	Twf1 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [TWF1_MOUSE] Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Actin dynamics provide the driving force for many cellular processes including motility and endocytosis. Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, and twinfilin, which sequesters actin monomers and caps filament barbed ends. Both interact with actin through an ADF homology (ADF-H) domain, which is also found in several other actin-binding proteins. However, in the absence of an atomic structure for the ADF-H domain in complex with actin, the mechanism by which these proteins interact with actin has remained unknown. Here, we present the crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer. This domain binds between actin subdomains 1 and 3 through an interface that is conserved among ADF-H domain proteins. Based on this structure, we suggest a mechanism by which ADF/cofilin and twinfilin inhibit nucleotide exchange of actin monomers and present a model for how ADF/cofilin induces filament depolymerization by weakening intrafilament interactions.

Structure of the actin-depolymerizing factor homology domain in complex with actin.,Paavilainen VO, Oksanen E, Goldman A, Lappalainen P J Cell Biol. 2008 Jul 14;182(1):51-9. PMID:18625842^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Beeler JF, Patel BK, Chedid M, LaRochelle WJ. Cloning and characterization of the mouse homolog of the human A6 gene. Gene. 1997 Jul 1;193(1):31-7. PMID:9249064
↑ Vartiainen M, Ojala PJ, Auvinen P, Peranen J, Lappalainen P. Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol Cell Biol. 2000 Mar;20(5):1772-83. PMID:10669753
↑ Falck S, Paavilainen VO, Wear MA, Grossmann JG, Cooper JA, Lappalainen P. Biological role and structural mechanism of twinfilin-capping protein interaction. EMBO J. 2004 Aug 4;23(15):3010-9. Epub 2004 Jul 29. PMID:15282541 doi:http://dx.doi.org/10.1038/sj.emboj.7600310
↑ Helfer E, Nevalainen EM, Naumanen P, Romero S, Didry D, Pantaloni D, Lappalainen P, Carlier MF. Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility. EMBO J. 2006 Mar 22;25(6):1184-95. Epub 2006 Mar 2. PMID:16511569 doi:http://dx.doi.org/7601019
↑ Paavilainen VO, Oksanen E, Goldman A, Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol. 2008 Jul 14;182(1):51-9. PMID:18625842 doi:10.1083/jcb.200803100

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3daw"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3daw]] is a 2 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=3DAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DAW FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a42|2a42]], [[2hd7|2hd7]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a42|2a42]], [[2hd7|2hd7]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Twf1 ([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">Twf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3daw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3daw RCSB], [http://www.ebi.ac.uk/pdbsum/3daw 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=3daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3daw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3daw RCSB], [http://www.ebi.ac.uk/pdbsum/3daw 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/TWF1_MOUSE TWF1_MOUSE]] Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.<ref>PMID:9249064</ref> <ref>PMID:10669753</ref> <ref>PMID:15282541</ref> <ref>PMID:16511569</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 37: @@
 [[Category: Mus musculus]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Goldman, A.]]
+[[Category: Goldman, A]]
-[[Category: Lappalainen, P.]]
+[[Category: Lappalainen, P]]
-[[Category: Oksanen, E.]]
+[[Category: Oksanen, E]]
-[[Category: Paavilainen, V O.]]
+[[Category: Paavilainen, V O]]
 [[Category: Actin binding protein]]
 [[Category: Actin depolymerisation]]

3daw

From Proteopedia

Revision as of 12:10, 25 December 2014

Structure of the actin-depolymerizing factor homology domain in complex with actin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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