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  • Title: Novel structural insights into F-actin-binding and novel functions of calponin homology domains.
    Author: Sjöblom B, Ylänne J, Djinović-Carugo K.
    Journal: Curr Opin Struct Biol; 2008 Dec; 18(6):702-8. PubMed ID: 18952167.
    Abstract:
    Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alpha-helical leucin-aspartate rich motif from paxillin.
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