PMID: 7013830Apr 1, 1981Paper

Symmetry and asymmetry in the contractile protein myosin

Biochimie
M C Schaub, J G Watterson

Abstract

The subunit composition of the myosin molecule which is built up from 3 pairs of identical polypeptide chains (2 heavy chains and 2 pairs of light chains), gives it the appearance of having symmetric structure. This homodimeric arrangement in the molecule is in fact asymmetric in its construction as a result of the natural folding of the chains. There are also heterodimers which result from combinations of pairs of heavy chains and/or light chains which are not identical in their amino acid sequence. Enzyme kinetics and ligand binding are characterised by homogeneous processes in studies on isolated myosin heads. With the double-headed molecular species, myosin and its water-soluble fragment heavy meromyosin, the enzyme kinetics, nucleotide and metal ion binding exhibit negative cooperativity. Binding of Mg-ADP to active centres induces site-site and therefore head-head interaction, thus intact myosin is designed to be able to function asymmetrically. It is suggested that the ligand-induced asymmetry between the heads plays a central role in crossbridge function. The two heads, even in rest, adopt non-equivalent conformations and it is argued that this built-in constraint complements the asymmetric mode of interaction they subs...Continue Reading

References

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