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1wm4

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Revision as of 16:21, 27 October 2021

Solution structure of mouse coactosin, an actin filament binding protein

Structural highlights

1wm4 is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COTL1_MOUSE] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.^[1]

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

Coactosin is a small (MW approximately 15 kDa) evolutionarily conserved actin filament binding protein. It displays remote sequence homology to ADF/cofilin proteins and to the ADF-H domains of twinfilin and Abp1/drebrin. However, biochemical analyses have demonstrated that coactosin has a very different role in actin dynamics from the ones of ADF/cofilin, twinfilin or Abp1/drebrin. To elucidate the molecular mechanism of coactosin/actin interaction, we determined the three-dimensional structure of mouse coactosin by multidimensional NMR spectroscopy. We find that the coactosin structure is homologous to ADF/cofilin and to the ADF-H domains of twinfilin. Furthermore, the regions that have been shown to be important for actin filament interactions in ADF/cofilins are structurally conserved in coactosin suggesting that these two proteins interact with F-actin through a conserved interface. Our analysis also identifies key structural differences between these proteins that may account for the differences in biochemical activities and cellular roles of these proteins.

Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins.,Hellman M, Paavilainen VO, Naumanen P, Lappalainen P, Annila A, Permi P FEBS Lett. 2004 Oct 8;576(1-2):91-6. PMID:15474017^[2]

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

References

↑ Doucet J, Provost P, Samuelsson B, Radmark O. Molecular cloning and functional characterization of mouse coactosin-like protein. Biochem Biophys Res Commun. 2002 Jan 18;290(2):783-9. PMID:11785969 doi:http://dx.doi.org/10.1006/bbrc.2001.6236
↑ Hellman M, Paavilainen VO, Naumanen P, Lappalainen P, Annila A, Permi P. Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins. FEBS Lett. 2004 Oct 8;576(1-2):91-6. PMID:15474017 doi:10.1016/j.febslet.2004.08.068

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wm4"

@@ Line 3: / Line 3: @@
 <StructureSection load='1wm4' size='340' side='right'caption='[[1wm4]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wm4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WM4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WM4 FirstGlance]. <br>
-</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=1wm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wm4 OCA], [http://pdbe.org/1wm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wm4 RCSB], [http://www.ebi.ac.uk/pdbsum/1wm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wm4 ProSAT]</span></td></tr>
+</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=1wm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wm4 OCA], [https://pdbe.org/1wm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wm4 RCSB], [https://www.ebi.ac.uk/pdbsum/1wm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wm4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/COTL1_MOUSE COTL1_MOUSE]] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.<ref>PMID:11785969</ref>
+[[https://www.uniprot.org/uniprot/COTL1_MOUSE COTL1_MOUSE]] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.<ref>PMID:11785969</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1wm4

From Proteopedia

Revision as of 16:21, 27 October 2021

Solution structure of mouse coactosin, an actin filament binding protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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