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Divalent Cations, Nucleotides, and Actin Structure

  • Chapter
Molecular Interactions of Actin

Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 32))

Abstract

Actin has one high-affinity site for a divalent cation, with a Kd for Ca2+ and Mg2+ in the nanomolar range. This binding site is located at the bottom of the cleft between the two domains of the molecule (Fig. 1). The cation is coordinated not only by amino acid residues but also by the oxygen of the γ- and/or β- phosphate groups of the nucleotide, ADP or ATP respectively, which is bound further up in the cleft (Valentin-Ranc and Carlier 1989; Kabsch et al. 1990). The tightly bound cation of G-actin exchanges with other divalent cations by a simple competitive mechanism.

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Authors and Affiliations

  1. Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093, Warsaw, Poland

    Hanna Strzelecka-Gołaszewska

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  1. Hanna Strzelecka-Gołaszewska
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  1. Department of Anatomy and Histology, Institute for Biomedical Research, University of Sydney, 2006, Sydney, Australia

    Cristobal G. dos Remedios

  2. Department of Biochemistry, University of Minnesota, 55455, Minneapolis, MN, USA

    David D. Thomas

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Strzelecka-Gołaszewska, H. (2001). Divalent Cations, Nucleotides, and Actin Structure. In: dos Remedios, C.G., Thomas, D.D. (eds) Molecular Interactions of Actin. Results and Problems in Cell Differentiation, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46560-7_3

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  • DOI: https://doi.org/10.1007/978-3-540-46560-7_3

  • Publisher Name: Springer, Berlin, Heidelberg

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