Ligand-Binding Sites on Calmodulin

  • H. J. Vogel
Part of the Handbook of Experimental Pharmacology book series (HEP, volume 83)


Calcium plays a pivotal role as an intracellular messenger in all eukaryotic cells. In resting cells the Ca2+ level is kept as low as 10–7 M. A series of membrane-bound exchange proteins and ATP-driven pump proteins are responsible for excreting the Ca2+ into the extracellular environment or into intracellular organelles that function as calcium stores. Taken together, these proteins produce a 10 000-fold gradient of Ca2+ over the plasma membrane, thus creating a situation that lends itself to a regulatory function (Rasmussen 1983). A hormonal or nerval impulse can generate an influx of Ca2+ into the cytoplasm through the calcium channels. This influx gives rise to a transiently increased Ca2+ level inside the cell. Although the Ca2+ concentration in an activated cell may differ widely between various cell types, it is generally around 10–6 M, which represents a tenfold increase from the resting level of 10–7 M (Rasmussen 1983). This situation is schematically depicted in Fig. 1. As a second step, the transient increase in intracellular Ca2+ needs to be translated into metabolic or contractile responses. To this end, nature has deployed a unique class of calcium-binding proteins. Upon binding Ca2+ they undergo a large conformational change which allows them to interact with and activate specific target proteins. For example, in skeletal and cardiac muscles the protein troponin C is the calcium-binding component which triggers contraction. In smooth muscle tissues the homologous protein calmodulin (CaM) is responsible for the Ca2+ triggering of the initiation of contraction (see Chap. 3).


Myosin Light Chain Kinase Proteolytic Fragment Cyclic Nucleotide Phosphodiesterase Calmodulin Antagonist Tryptic Fragment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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© Springer-Verlag Berlin Heidelberg 1988

Authors and Affiliations

  • H. J. Vogel

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