Sandbox Reserved 825: Difference between revisions
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The FKBP12-rapamycin binding (FRB) domain mediates ligand-dependent regulation of the kinase domain by binding different molecules. | The FKBP12-rapamycin binding (FRB) domain mediates ligand-dependent regulation of the kinase domain by binding different molecules. | ||
FRB binds the inhibitory cyclic macroloide '''rapamycin''' in complex with the small '''peptidyl-prolyl cis-trans isomerase [http://en.wikipedia.org/wiki/FKBP FKBP12]''' leading to a decreased activity of the kinase domain. Due to its inhibitory effect rapamycin has been a widely used tool for studying mTOR. <br />FRB is also capable of binding '''the activator [http://en.wikipedia.org/wiki/Phosphatidic_acid phosphatidic acid]''' and small molecules, for example amino acids like '''[http://en.wikipedia.org/wiki/Leucine leucine]'''. <ref> Russell, R. C., Fang, C., & Guan, K. L. (2011). An emerging role for TOR signaling in mammalian tissue and stem cell physiology. Development, 138(16), 3343-3356. </ref> | FRB binds the inhibitory cyclic macroloide '''rapamycin''' in complex with the small '''peptidyl-prolyl cis-trans isomerase [http://en.wikipedia.org/wiki/FKBP FKBP12]''' leading to a decreased activity of the kinase domain. Due to its inhibitory effect rapamycin has been a widely used tool for studying mTOR. <br />FRB is also capable of binding '''the activator [http://en.wikipedia.org/wiki/Phosphatidic_acid phosphatidic acid]''' and small molecules, for example amino acids like '''[http://en.wikipedia.org/wiki/Leucine leucine]'''. <ref> Russell, R. C., Fang, C., & Guan, K. L. (2011). An emerging role for TOR signaling in mammalian tissue and stem cell physiology. Development, 138(16), 3343-3356. doi: http://dev.biologists.org/content/138/16/3343.full </ref> | ||
