Sandbox Reserved 479: Difference between revisions
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====Active Site==== | ====Active Site==== | ||
The actin-binding, catalytic site of myosin is known as S1 (subfragment 1). This is the amino-terminal globular head portion of the myosin molecule. The S1 head is divided into three subdomains: the NH2-terminal 25 kDa region, a central 50 kDa region, and the COOH-terminal 20 kDa region. Further analysis of the S1 active site of myosin suggests that the γ-phosphate (of ATP) binds near the apex of the 50 kDa cleft. It is believed to be a region critical to function, because of the presence of evolutionarily conserved residues along the central cleft.<ref name="Ruppel" /> | The actin-binding, catalytic site of myosin is known as S1 (subfragment 1). This is the amino-terminal globular head portion of the myosin molecule. The S1 head is divided into three subdomains: the NH2-terminal 25 kDa region, a central 50 kDa region, and the COOH-terminal 20 kDa region. Further analysis of the S1 active site of myosin suggests that the γ-phosphate (of ATP) binds near the apex of the 50 kDa cleft. It is believed to be a region critical to function, because of the presence of evolutionarily conserved residues along the central cleft.<ref name="Ruppel" /> The actin-binding site and nucleotide-binding site, although dominated by alpha-helices, also contains a straightened section with two cysteine residues. The can form a disulfide bond in the presence of a nucleotide that prevents ADP from leaving the active site. | ||
====Ligands==== | ====Ligands==== | ||
