Collagen receptor on fibroblasts, endotelial cells and macrophages. Vogel, W.F., 2001. Collagen-receptor signaling in health and disease. European Journal of Dermatology 11, 506-514. White, D.J., Puranen, S., Johnson, M.S., Heino, J., 2004. The collagen receptor subfamily of the integrins. International Journal of Biochemistry & Cell Biology 36, 1405-1410. Collagen receptor Collagen receptors are membrane proteins that bind the extracellular matrix protein collagen, the most abundant protein in mammals. They control mainly cell proliferation, migration and adhesion, coagulation cascade activation and they affect ECM structure by regulation of MMP (matrix metalloproteinases). There are at least eight human collagen receptors belonging to four different
Myosin domain. Multiple myosin II molecules generate force in skeletal muscle through a power stroke mechanism fuelled by the energy released from ATP hydrolysis. The power stroke occurs at the release of phosphate from the myosin molecule after the ATP hydrolysis while myosin is tightly bound to actin. The effect of this release is a conformational change in the molecule that pulls against the actin. The release of the ADP molecule leads to the so-called rigor state of myosin. The binding of a new ATP molecule will release myosin from actin. ATP hydrolysis within the myosin will cause it to bind