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.


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Elizabeth Schilling, Michal Harel