Myosin: Difference between revisions
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{{STRUCTURE_3i5f| PDB=3i5f | SIZE=400| SCENE= |right|CAPTION=Squid myosin: heavy chain (grey), regulatory light chain (green), catalytic light chain (pink) complex with ADP (stick model) and Mg+2 ion (green) [[3i5f]] }} | {{STRUCTURE_3i5f| PDB=3i5f | SIZE=400| SCENE= |right|CAPTION=Squid myosin II: heavy chain (grey), regulatory light chain (green), catalytic light chain (pink) complex with ADP (stick model) and Mg+2 ion (green) [[3i5f]] }} | ||
== Introduction == | == Introduction == | ||
[[Myosin]] is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref> Myosin is a superfamily of proteins which bind actin, hydrolyze ATP and transduce force. Thus most are located in muscle cells. Composed of head, neck and tail domains. Head domain binds the actin and moves along it. The neck is a linker and binds the light chains which have a regulatory function. The tail interacts with cargo molecules (CBD)m. There are 18 classes of myosin.<br /> | [[Myosin]] is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref> Myosin is a superfamily of proteins which bind actin, hydrolyze ATP and transduce force. Thus most are located in muscle cells. Composed of head, neck and tail domains. Head domain binds the actin and moves along it. The neck is a linker and binds the light chains which have a regulatory function. The tail interacts with cargo molecules (CBD)m. There are 18 classes of myosin.<br /> | ||