1yv3
From Proteopedia
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|PDB= 1yv3 |SIZE=350|CAPTION= <scene name='initialview01'>1yv3</scene>, resolution 2.0Å | |PDB= 1yv3 |SIZE=350|CAPTION= <scene name='initialview01'>1yv3</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BIT:(-)-1-PHENYL-1,2,3,4-TETRAHYDRO-4-HYDROXYPYRROLO[2,3-B]-7-METHYLQUINOLIN-4-ONE'>BIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1vom|1VOM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yv3 OCA], [http://www.ebi.ac.uk/pdbsum/1yv3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yv3 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
[[Category: Smith, R.]] | [[Category: Smith, R.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: BIT]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: VO4]] | ||
[[Category: blebbistatin]] | [[Category: blebbistatin]] | ||
[[Category: metastable state]] | [[Category: metastable state]] | ||
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[[Category: myosin-inhibitor complex]] | [[Category: myosin-inhibitor complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:23:38 2008'' |
Revision as of 22:23, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Related: | 1VOM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The structural basis of blebbistatin inhibition and specificity for myosin II
Overview
Molecular motors play a central role in cytoskeletal-mediated cellular processes and thus present an excellent target for cellular control by pharmacological agents. Yet very few such compounds have been found. We report here the structure of blebbistatin, which inhibits specific myosin isoforms, bound to the motor domain of Dictyostelium discoideum myosin II. This reveals the structural basis for its specificity and provides insight into the development of new agents.
About this Structure
1YV3 is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
The structural basis of blebbistatin inhibition and specificity for myosin II., Allingham JS, Smith R, Rayment I, Nat Struct Mol Biol. 2005 Apr;12(4):378-9. Epub 2005 Mar 6. PMID:15750603
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