1WM4

Solution structure of mouse coactosin, an actin filament binding protein

Summary for 1WM4

• Entry DOI: 10.2210/pdb1wm4/pdb
• NMR Information: BMRB: 6032
• Descriptor: Coactosin-like protein (1 entity in total)
• Functional Keywords: adf-h domain, protein binding
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm, cytoskeleton (By similarity): Q9CQI6
• Total number of polymer chains: 1
• Total formula weight: 15964.90

Authors

Hellman, M.,Paavilainen, V.O.,Naumanen, P.,Lappalainen, P.,Annila, A.,Permi, P. (deposition date: 2004-07-03, release date: 2004-11-02, Last modification date: 2024-05-29)

Primary citation

Hellman, M.,Paavilainen, V.O.,Naumanen, P.,Lappalainen, P.,Annila, A.,Permi, P.
Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins
Febs Lett., 576:91-96, 2004

PubMed 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.

PubMed: 15474017
DOI: 10.1016/j.febslet.2004.08.068

Experimental method

SOLUTION NMR