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  • Title: Role of ATP in the binding of caldesmon to smooth muscle myosin.
    Author: Lu FW, Chalovich JM.
    Journal: Biochemistry; 1995 May 16; 34(19):6359-65. PubMed ID: 7756264.
    Abstract:
    We have reported earlier that ATP causes both an increase in the affinity of caldesmon for smooth muscle myosin and a change in stoichiometry from 2 caldesmon molecules per myosin to 1:1 (Hemric & Chalovich, 1990). We now show that this ATP effect does not occur with skeletal muscle myosin, indicating that ATP has a specific effect on the structure of filamentous smooth muscle myosin. This ATP effect does not appear to be due to stabilization of a 10S type of filamentous smooth muscle myosin like that reported earlier (Ikebe & Hartshorne, 1984) since neither phosphorylation nor extensive modification of myosin with MalNEt (both which stabilize the 6S state of monomeric myosin) eliminates the effect of ATP. Caldesmon does bind more tightly to a form of smooth muscle myosin which is resistant to papain digestion. These results suggest that the ATP effect is due to stabilization of a local conformation of smooth muscle myosin which is independent of the larger 10S/6S conformational change (Suzuki et al., 1988). In the presence of ATP, the two heads of smooth muscle muscle myosin and the S-2 region form a single, higher affinity binding region for caldesmon.
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