Sandbox Reserved 825

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	=='''FRB Domain'''==		=='''FRB Domain'''==
-	mTOR is highly conserved across all eukaryotes, with 40–60% amino-acid sequence identity.	+	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 (or '''2NPU''')
-	mTOR contains a number of distinct functional domains including up to''' The FRB domain''' of '''mTOR''' (or '''2NPU''') which is responsible for the binding of the inhibitory cyclic macrolide '''Rapamycin'''	+	mTOR is highly conserved across all eukaryotes, with 40–60% amino-acid sequence identity.

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Revision as of 13:24, 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: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

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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 (or 2NPU)

mTOR is highly conserved across all eukaryotes, with 40–60% amino-acid sequence identity.