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Sandbox GGC3
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== Function == | == Function == | ||
| - | Myosin is a type of motor protein, which are proteins that specialize in turning Chemical Energy to mechanical Energy. The protein is commonly found in muscle tissue and is used for motility in eukaryotes. In order for the process to work, myosin uses the subdomains in its head to locate and attach to actin filaments.ATP is brought into the myosin active site, where ATPase hydrolyze the ATP to ADP+Pi.The hydrolyzing leads to tighter binding of the myosin and actin filament.The release of the Pi also leads to even tighter binding.The binding of myosin and actin filament forms what is known as muscle contraction or simply contractions.An additional ATP can be added to the structure to release the actin and have the cycle repeated. | + | Myosin is a type of motor protein, which are proteins that specialize in turning Chemical Energy to mechanical Energy. The protein is commonly found in muscle tissue and is used for motility in eukaryotes. In order for the process to work, myosin uses the subdomains in its head to locate and attach to actin filaments.ATP is brought into the myosin active site, where ATPase hydrolyze the ATP to ADP+Pi.The hydrolyzing leads to tighter binding of the myosin and actin filament.The release of the Pi also leads to even tighter binding. (3) The binding of myosin and actin filament forms what is known as muscle contraction or simply contractions.An additional ATP can be added to the structure to release the actin and have the cycle repeated. (1) |
== Disease == | == Disease == | ||
| - | Common disease related to myosin is Myosin Storage Myopathy or Myopathy for short, which leads to muscle weakness. The is due to mutation of the MYH7 gene that synthesizes the long heavy chain. The mutation causes clumping of the myosin protein. The clumping | + | Common disease related to myosin is Myosin Storage Myopathy or Myopathy for short, which leads to muscle weakness.(2) The is due to mutation of the MYH7 gene that synthesizes the long heavy chain. The mutation causes clumping of the myosin protein. The clumping |
stops the myosin from gathering filaments to create good contractions. The lack of this may be leading to the muscle weakness but it still unclear. | stops the myosin from gathering filaments to create good contractions. The lack of this may be leading to the muscle weakness but it still unclear. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | <scene name='75/752266/Stop_scene_of_1b7t_top/1'>This scene represents zoomed in view of the labeled myosin</scene> The labels are the amino acids that make up the subunits of the myosin. Switch(Ile461-Asn470) is orange, Relay (Asn489-Asp515) is yellow, Sh1 helix(Cys693-Phe707) is cyan, Converter (707-774) is lime and the Long Heavy Chain (775-835) is black. <scene name='75/752266/1b7t_long_chain/2'>The long heavy chain of myosin</scene> <scene name='75/752266/Myosin_ball_and_stick_view/2'>This is a ball and stick model of myosin, with the head removed to identify subunits better.</scene> The colors of the label match up to the same labeling used for the ribbon model. <scene name='75/752266/Myosin_actinattachment/1'>Overhead view of the myosin head, where the actin filament will enter.</scene> | + | <scene name='75/752266/Stop_scene_of_1b7t_top/1'>This scene represents zoomed in view of the labeled myosin</scene> The labels are the amino acids that make up the subunits of the myosin. Switch(Ile461-Asn470) is orange, Relay (Asn489-Asp515) is yellow, Sh1 helix(Cys693-Phe707) is cyan, Converter (707-774) is lime and the Long Heavy Chain (775-835) is black. <scene name='75/752266/1b7t_long_chain/2'>The long heavy chain of myosin</scene> <scene name='75/752266/Myosin_ball_and_stick_view/2'>This is a ball and stick model of myosin, with the head removed to identify subunits better.</scene> The colors of the label match up to the same labeling used for the ribbon model. <scene name='75/752266/Myosin_actinattachment/1'>Overhead view of the myosin head, where the actin filament will enter.</scene> (1) |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| - | AnneHoudusse, Vassilios N.Kalabokis, DanielHimmel, Andrew G.Szent-Györgyi, CarolynCohen "Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP: A Novel Conformation of the Myosin Head":https://www.sciencedirect.com/science/article/pii/S0092867400807564 <references/> | + | (1) AnneHoudusse, Vassilios N.Kalabokis, DanielHimmel, Andrew G.Szent-Györgyi, CarolynCohen "Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP: A Novel Conformation of the Myosin Head":https://www.sciencedirect.com/science/article/pii/S0092867400807564 <references/> |
| - | https://en.wikibooks.org/wiki/Structural_Biochemistry/Protein_function/Myosin | + | |
| - | https://ghr.nlm.nih.gov/condition/myosin-storage-myopathy#genes | + | (2) https://en.wikibooks.org/wiki/Structural_Biochemistry/Protein_function/Myosin |
| + | |||
| + | (3) https://ghr.nlm.nih.gov/condition/myosin-storage-myopathy#genes | ||
Revision as of 13:50, 20 November 2019
Structure of Scallop Myosin 1b7t
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References
(1) AnneHoudusse, Vassilios N.Kalabokis, DanielHimmel, Andrew G.Szent-Györgyi, CarolynCohen "Atomic Structure of Scallop Myosin Subfragment S1 Complexed with MgADP: A Novel Conformation of the Myosin Head":https://www.sciencedirect.com/science/article/pii/S0092867400807564
(2) https://en.wikibooks.org/wiki/Structural_Biochemistry/Protein_function/Myosin
(3) https://ghr.nlm.nih.gov/condition/myosin-storage-myopathy#genes
