1wm4
From Proteopedia
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Solution structure of mouse coactosin, an actin filament binding protein
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.
About this Structure
1WM4 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 05:31:31 2007
