Key result
This paper reviews procedures for analyzing the interactions of caldesmon with actin and myosin, summarizing its stability, dynamics, and possible effects on transitions within the ATPase cycle.
This paper reviews the mechanisms by which caldesmon interacts with actin and myosin to inhibit actin-activated myosin ATPase activity.
Answers are grounded in this paper and cite their sources.
No clinical application yet from caldesmon mechanisms; leaves open targeted vascular research.
The actin binding protein caldesmon inhibits the actin-activation of myosin ATPase activity. The steps in the cycle of ATP hydrolysis that caldesmon could inhibit include: (1) the binding of myosin to actin, (2) the transition between any two actin-myosin states and (3) the distribution between inactive and active states of actin. The analysis of these possibilities is complicated because caldesmon binds to both myosin and actin and because each caldesmon molecule binds to several actin monomers. This paper reviews procedures for analysing these interactions and summarizes current information on the stability and dynamics of the interaction of caldesmon with actin and myosin. Possible effects of caldesmon on transitions within the ATPase cycle of actomyosin are also discussed.
No takes yet. Share an insight, caveat, or question.
Chalovich et al. (1998) reported a review. Caldesmon was evaluated. This paper reviews procedures for analyzing the interactions of caldesmon with actin and myosin, summarizing its stability, dynamics, and possible effects on transitions within the ATPase cycle.
Synapse has enriched 10 related papers. Consider them for comparative context: