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Sandbox ggc6
From Proteopedia
(Difference between revisions)
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== Relevance == | == Relevance == | ||
| - | Carboxamide 22 potentially possess two different binding modes: allosteric binding and hinge binding. This hypothesis was also supported by the fact that FAK inhibitory potential of compound 22 under the high concentration of ATP was much weaker. The purpose was to facilitate pure allosteric inhibition of FAK by targeting FAK allosteric site, demonstrating a potential of FAK allosteric inhibitors as antitumor agents. | + | Carboxamide 22 potentially possess two different binding modes: allosteric binding and hinge binding. This hypothesis was also supported by the fact that FAK inhibitory potential of compound 22 under the high concentration of ATP was much weaker. The purpose was to facilitate pure allosteric inhibition of FAK by targeting the FAK allosteric site, demonstrating a potential of FAK allosteric inhibitors as antitumor agents. |
== Structural highlights == | == Structural highlights == | ||
<scene name='75/752265/Transferase/8'>Overview of Transferase Structure</scene>. The CPK ligand (22) forms direct and/or water-mediated hydrogen bonds with Glu506, Ser509, and Arg514. These three sites are shown and labeled within the structure. | <scene name='75/752265/Transferase/8'>Overview of Transferase Structure</scene>. The CPK ligand (22) forms direct and/or water-mediated hydrogen bonds with Glu506, Ser509, and Arg514. These three sites are shown and labeled within the structure. | ||
Revision as of 20:36, 10 April 2017
Transferase/Transferase Inhibitor
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
