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: 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. Myosin II (MII) is best studied and contains 2 heavy chains (HC)  which constitute the head or motor domain (MD) and the tail domain and 4 light chains (LC) which are referred to as the essential LC (ELC) and the regulatory LC (RLC).  
[[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 II''' (MII) is best studied.  It drives high-speed motility like muscle contraction.  MII contains 2 heavy chains (HC)  which constitute the head or motor domain (MD) and the tail domain and 4 light chains (LC) which are referred to as the essential LC (ELC) and the regulatory LC (RLC). <br />
*'''Myosin V''' (MV) works with microtubule based motors like kinesin<ref>PMID:10448864</ref>.
*'''Myosin VI''' (MVI) moves toward the minus end of the actin filament<ref>PMID:15473855</ref>.
*'''Myosin X''' (MX) is a downstream effector of PI(3)K during phagocytosis<ref>PMID:12055636</ref>.


==Crystallization and X-ray diffraction==
==Crystallization and X-ray diffraction==
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**[[3dtp]] - RLC+HC+ELC – tarantula – Cryo EM
**[[3dtp]] - RLC+HC+ELC – tarantula – Cryo EM
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==Literature Cited==
== References ==
<references/>
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

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Laurel Koopmans, David Canner, Alexander Berchansky, Michal Harel, Jaime Prilusky, Joel L. Sussman