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| + | = FKBP12-rapamycin binding domain of mTOR = | ||
''' FRB domain''' of '''mTOR''' (or '''2NPU''') is responsible for the binding of the inhibitory cyclic macrolide '''Rapamycin''' | ''' FRB domain''' of '''mTOR''' (or '''2NPU''') is responsible for the binding of the inhibitory cyclic macrolide '''Rapamycin''' | ||
| - | = | + | == Introduction == |
| - | + | As a member of the phosphatidylinositol kinase-related kinases(PIKK)* the mammalian targert of rapamycin (mTOR)* | |
| + | is a multi domain protein which is involved in the regulation of cell growth and an important target of survival | ||
| + | signals. The sequence of 2549 residues is highly conserved across eukaryotes (40-60% precent sequence identity). | ||
| + | The protein consists of several functional domains: At the N-terminus there are 12 HEAT* repeats followed by a | ||
| + | central FAT* domain (residue 1513 - 1910), a FRB domain (residue 2015 - 2114) a serine-threonine kinase domain | ||
| + | (residue 2181 - 2484) and a C-terminal FATC* domain (residue 2515 - 2549). | ||
| + | The FKBP12-rapamycin binding (FRB) domain binds the inhibitory cyclic macroloide* rapamycin in complex with the | ||
| + | small peptidyl-prolyl cis-trans isomerase 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. | ||
| + | FRB is also capable of binding the activator phosphatidic acid* and small molecules, for example amino acids like | ||
| + | leucine. | ||
<Structure load='2npu' size='300' frame='true' align='right' caption='Cartoon model of the FRB domain of mTOR' scene='56/568023/2npu_cartoon_rainbow/1' /> | <Structure load='2npu' size='300' frame='true' align='right' caption='Cartoon model of the FRB domain of mTOR' scene='56/568023/2npu_cartoon_rainbow/1' /> | ||
Revision as of 12:28, 1 January 2014
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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FKBP12-rapamycin binding domain of mTOR
FRB domain of mTOR (or 2NPU) is responsible for the binding of the inhibitory cyclic macrolide Rapamycin
Introduction
As a member of the phosphatidylinositol kinase-related kinases(PIKK)* the mammalian targert of rapamycin (mTOR)* is a multi domain protein which is involved in the regulation of cell growth and an important target of survival signals. The sequence of 2549 residues is highly conserved across eukaryotes (40-60% precent sequence identity). The protein consists of several functional domains: At the N-terminus there are 12 HEAT* repeats followed by a central FAT* domain (residue 1513 - 1910), a FRB domain (residue 2015 - 2114) a serine-threonine kinase domain (residue 2181 - 2484) and a C-terminal FATC* domain (residue 2515 - 2549). The FKBP12-rapamycin binding (FRB) domain binds the inhibitory cyclic macroloide* rapamycin in complex with the small peptidyl-prolyl cis-trans isomerase 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. FRB is also capable of binding the activator phosphatidic acid* and small molecules, for example amino acids like leucine.
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Residues of FRB
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And now let us try to implement a scence that highlights the of the alpha 1 and alpha 4 helices of the FRB domain
