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An open or closed case for the conformation of calponin homology domains on F-actin?

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Abstract

Calponin homology domains link many different proteins to the surface of actin filaments. However, details of the structural interactions involved and the methods used to determine them are controversial. In the case of the actin-binding protein utrophin, for example, several models have been proposed for the binding of utrophin's calponin homology domains to actin. We review and evaluate these models and their supporting data.

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Authors and Affiliations

  1. Department of Physiology and Biophysics, Boston University School of Medicine, 715 Albany Street, MA, USA

    William Lehman

  2. Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, MA, USA

    Roger Craig

  3. Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, UK

    John Kendrick-Jones

  4. Institute of Molecular BioSciences, Massey University, Private Bag, 11222, New Zealand

    Andrew J. Sutherland-Smith

Authors
  1. William Lehman
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  2. Roger Craig
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  3. John Kendrick-Jones
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  4. Andrew J. Sutherland-Smith
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Lehman, W., Craig, R., Kendrick-Jones, J. et al. An open or closed case for the conformation of calponin homology domains on F-actin?. J Muscle Res Cell Motil 25, 351–358 (2004). https://doi.org/10.1007/s10974-004-0690-7

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  • DOI: https://doi.org/10.1007/s10974-004-0690-7

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