1wm4: Difference between revisions

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[[Image:1wm4.jpg|left|200px]]<br /><applet load="1wm4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1wm4.jpg|left|200px]]<br /><applet load="1wm4" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1wm4" />

'''Solution structure of mouse coactosin, an actin filament binding protein'''<br />

==Overview==

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.

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.

==About this Structure==

1WM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WM4 OCA].

1WM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WM4 OCA].

==Reference==

Line 17:

[[Category: Lappalainen, P.]]

[[Category: Naumanen, P.]]

[[Category: Paavilainen, V.O.]]

[[Category: Paavilainen, V O.]]

[[Category: Permi, P.]]

[[Category: adf-h domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 05:31:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:52 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1wm4.jpg|left|200px]]<br /><applet load="1wm4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wm4.jpg|left|200px]]<br /><applet load="1wm4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wm4" />
 '''Solution structure of mouse coactosin, an actin filament binding protein'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-WM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WM4 OCA].
+WM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WM4 OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Lappalainen, P.]]
 [[Category: Naumanen, P.]]
-[[Category: Paavilainen, V.O.]]
+[[Category: Paavilainen, V O.]]
 [[Category: Permi, P.]]
 [[Category: adf-h domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:31:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:52 2008''