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' 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. Troponin is a trimeric complex of three proteins (I, T, and C), each with a different function that allows troponin to perform its role relating to muscle contraction. | |||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||