We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Sandbox Reserved 825
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
=='''FRB Domain'''== | =='''FRB Domain'''== | ||
| - | The mammalian target of rapamycin ('''mTOR''') is a protein that is intricately involved in signaling pathways controlling cell growth. '''Rapamycin''' is a natural product that binds and inhibits mTOR function by interacting with its '''FKBP-rapamycin-binding (FRB) domain''' | + | |
| + | The mammalian target of rapamycin ('''mTOR''') is a protein that is intricately involved in signaling pathways controlling cell growth. '''Rapamycin''' is a natural product that binds and inhibits mTOR function by interacting with its '''FKBP-rapamycin-binding (FRB) domain'''. | ||
mTOR is highly conserved across all eukaryotes, with 40–60% amino-acid sequence identity. | mTOR is highly conserved across all eukaryotes, with 40–60% amino-acid sequence identity. | ||
Revision as of 13:27, 30 December 2013
| 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. |
To get started:
More help: Help:Editing |
|
Contents |
FRB Domain
The mammalian target of rapamycin (mTOR) is a protein that is intricately involved in signaling pathways controlling cell growth. Rapamycin is a natural product that binds and inhibits mTOR function by interacting with its FKBP-rapamycin-binding (FRB) domain.
mTOR is highly conserved across all eukaryotes, with 40–60% amino-acid sequence identity.
