Sandbox10: Difference between revisions
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The portion of the protein that is shown is the motor domain of the heavy chain. This protein is largely composed of <scene name='Sandbox10/Helix/1'>alpha-helices</scene> connected by randomly oriented chains. There are also several areas of <scene name='Sandbox10/Betasheets/1'>beta-sheets</scene>, both parallel and anti-parallel. | The portion of the protein that is shown is the motor domain of the heavy chain. This protein is largely composed of <scene name='Sandbox10/Helix/1'>alpha-helices</scene> connected by randomly oriented chains. There are also several areas of <scene name='Sandbox10/Betasheets/1'>beta-sheets</scene>, both parallel and anti-parallel. | ||
This view shows the <scene name='Sandbox10/Newscene/2'>active sites</scene> of the protein with the ATP analog ADP-Metavanadate bound to one active site and the allosteric inhibitor pentabromopseudilin. | This view shows the <scene name='Sandbox10/Newscene/2'>active sites</scene> of the protein with the ATP analog ADP-Metavanadate bound to one active site and the allosteric inhibitor pentabromopseudilin. | ||
Myosin contains many <scene name='Sandbox10/Polar/1'>polar</scene> side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following <scene name='Sandbox10/Hydrophobic/1'>scene</scene> shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein. | Myosin contains many <scene name='Sandbox10/Polar/1'>polar</scene> side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following <scene name='Sandbox10/Hydrophobic/1'>scene</scene> shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein in a <scene name='Sandbox10/Hydrophobic/1'>space-filling view</scene> and a <scene name='Sandbox10/Polarnonpolar/1'>cartoon view</scene>. 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. | 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. | ||
{{STRUCTURE_2jhr | PDB=2jhr | SCENE= }} | {{STRUCTURE_2jhr | PDB=2jhr | SCENE= }} | ||
Revision as of 19:41, 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.
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 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 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.
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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 | ||||||||
