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Myosin II is found in the myofibers of skeletal, smooth, and cardiac muscle tissue where the protein forms the thick filaments. The myosin of the thick filaments has the ability to bind the thin filaments, composed of actin. The myosin head then rotates and pulls the two filaments past one another providing the basis for muscle contraction. | Myosin II is found in the myofibers of skeletal, smooth, and cardiac muscle tissue where the protein forms the thick filaments. The myosin of the thick filaments has the ability to bind the thin filaments, composed of actin. The myosin head then rotates and pulls the two filaments past one another providing the basis for muscle contraction. | ||
{{STRUCTURE_2jhr | PDB=2jhr | SCENE= }} | |||
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Thanks to Fedorov, R., Boehl, M., Tsiavaliaris, G., Hartmann, F.K., Baruch, P., Brenner, B., Martin, R., Knoelker, H.J., Gutzeit, H.O., Manstein, D.J. for their work in resolving the structure of this protein. | Thanks to Fedorov, R., Boehl, M., Tsiavaliaris, G., Hartmann, F.K., Baruch, P., Brenner, B., Martin, R., Knoelker, H.J., Gutzeit, H.O., Manstein, D.J. for their work in resolving the structure of this protein. | ||
Revision as of 19:51, 2 March 2009
ɓThis sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks! Brendan Jones
Myosin 2 Motor DomainMyosin 2 Motor Domain
Myosin is a protein known largely for it's involvement in the contraction of the body's muscles. However, this protein can also be found in the ears and eyes, blood platelets, and it has functions in cytokinesis.
Myosin II is found in the myofibers of skeletal, smooth, and cardiac muscle tissue where the protein forms the thick filaments. The myosin of the thick filaments has the ability to bind the thin filaments, composed of actin. The myosin head then rotates and pulls the two filaments past one another providing the basis for muscle contraction.
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| 2jhr, resolution 2.80Å () | |||||||||
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| Ligands: | , , | ||||||||
| Related: | 1mne, 1d1c, 1jx2, 1q5g, 1w9l, 1vom, 1d0y, 1mmn, 2aka, 1lvk, 1w9j, 1jwy, 1yv3, 1fmv, 1fmw, 1d0x, 1d1b, 1g8x, 1mma, 1d1a, 1mmg, 1w9i, 1d0z, 1mnd, 1w9k, 1mmd, 2jj9 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
The portion of the protein that is shown is the motor domain of the heavy chain. This protein is largely composed of connected by randomly oriented chains. There are also several areas of , both parallel and anti-parallel. This component of the protein represents only one part of the hexamer the makes up the entire mosin unit. In addition there is another heavy chain and four light chains. The tails of the two heavy chains, which can not be seen, coil about one another to form the thick filament. The four lights chains bind the myosin between the head and tail region, two light chain molecules per heavy chain. These light chains are known as the essential light chain and the regulatory light chain.
This view shows the of the protein with the ATP analog ADP-Metavanadate bound to one active site and the allosteric inhibitor pentabromopseudilin.
Myosin contains many side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following scene shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein in a and a . By looking at these scenes one can see that although hyrbrophobic molecules penetrate the surface of the molecule, there are no areas of high hydrophobic concentration.
Thanks to Fedorov, R., Boehl, M., Tsiavaliaris, G., Hartmann, F.K., Baruch, P., Brenner, B., Martin, R., Knoelker, H.J., Gutzeit, H.O., Manstein, D.J. for their work in resolving the structure of this protein.