Human Cardiac Troponin I: Difference between revisions
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== Introduction == | == Introduction == | ||
<StructureSection load='4Y99' size='340' side='right' caption='Core domain of human cardiac troponin' scene=''> | <StructureSection load='4Y99' size='340' side='right' caption='Core domain of human cardiac troponin (PDB code [[4y99]])' scene=''> | ||
The contraction of skeletal and cardiac muscle (striated muscle) is enabled when calcium ions bind to troponin, which causes a conformational change and pulls the tropomyosin off the myosin-binding sites on the actin filaments. The uncovering of the binding sites allows the myosin heads to bind the actin, forming a cross-bridge. Once ATP hydrolysis occurs, the power stroke needed for a muscle contraction pulls the actin and myosin filaments closer to the M line, shortening the sarcomere. <scene name='90/902741/Troponin/1'>Troponin</scene> is a trimeric complex of three proteins (<scene name='90/902741/Troponin_i/1'>I</scene>, <scene name='90/902741/Troponin_t/1'>T</scene>, and <scene name='90/902741/Troponin_c/1'>C</scene>), each with a different function that allows troponin to perform its role relating to muscle contraction. | The contraction of skeletal and cardiac muscle (striated muscle) is enabled when calcium ions bind to troponin, which causes a conformational change and pulls the tropomyosin off the myosin-binding sites on the actin filaments. The uncovering of the binding sites allows the myosin heads to bind the actin, forming a cross-bridge. Once ATP hydrolysis occurs, the power stroke needed for a muscle contraction pulls the actin and myosin filaments closer to the M line, shortening the sarcomere. <scene name='90/902741/Troponin/1'>Troponin</scene> is a trimeric complex of three proteins (<scene name='90/902741/Troponin_i/1'>I</scene>, <scene name='90/902741/Troponin_t/1'>T</scene>, and <scene name='90/902741/Troponin_c/1'>C</scene>), each with a different function that allows troponin to perform its role relating to muscle contraction. | ||