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Sandbox ggc6
From Proteopedia
(Difference between revisions)
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In order to develop potent and selective focal adhesion kinase (FAK) inhibitors, studies on pyrazolo[4,3-c][2,1]benzothiazines targeted for the FAK allosteric site were carried out <ref>DOI 10.1016/j.bmcl.2013.01.047</ref>. This compound potentially possess two different binding modes: allosteric binding and hinge binding, and 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. | In order to develop potent and selective focal adhesion kinase (FAK) inhibitors, studies on pyrazolo[4,3-c][2,1]benzothiazines targeted for the FAK allosteric site were carried out <ref>DOI 10.1016/j.bmcl.2013.01.047</ref>. This compound potentially possess two different binding modes: allosteric binding and hinge binding, and 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 (compound 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 (compound 22) forms direct and/or water-mediated hydrogen bonds with Glu506, Ser509, and Arg514. These three sites are shown and labeled within the structure. The water mediated Hydrogen bond formed with Glu506 is also shown within the structure. |
Color Key: | Color Key: | ||
Cyan-Alpha Helix; | Cyan-Alpha Helix; | ||
Revision as of 16:41, 17 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
- ↑ Tomita N, Hayashi Y, Suzuki S, Oomori Y, Aramaki Y, Matsushita Y, Iwatani M, Iwata H, Okabe A, Awazu Y, Isono O, Skene RJ, Hosfield DJ, Miki H, Kawamoto T, Hori A, Baba A. Structure-based discovery of cellular-active allosteric inhibitors of FAK. Bioorg Med Chem Lett. 2013 Mar 15;23(6):1779-85. doi: 10.1016/j.bmcl.2013.01.047., Epub 2013 Jan 26. PMID:23414845 doi:http://dx.doi.org/10.1016/j.bmcl.2013.01.047
- ↑ Tomita N, Hayashi Y, Suzuki S, Oomori Y, Aramaki Y, Matsushita Y, Iwatani M, Iwata H, Okabe A, Awazu Y, Isono O, Skene RJ, Hosfield DJ, Miki H, Kawamoto T, Hori A, Baba A. Structure-based discovery of cellular-active allosteric inhibitors of FAK. Bioorg Med Chem Lett. 2013 Mar 15;23(6):1779-85. doi: 10.1016/j.bmcl.2013.01.047., Epub 2013 Jan 26. PMID:23414845 doi:http://dx.doi.org/10.1016/j.bmcl.2013.01.047
