| Literature DB >> 15474017 |
Maarit Hellman1, Ville O Paavilainen, Perttu Naumanen, Pekka Lappalainen, Arto Annila, Perttu Permi.
Abstract
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. Copyright 2004 Federation of European Biochemical SocietiesEntities:
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Year: 2004 PMID： 15474017 DOI： 10.1016/j.febslet.2004.08.068
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124