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The surface structure reveals two main interaction sites, a shallow <scene name='56/568023/Hydrophobic_pocket/2'>hydrophobic patch</scene> made up of helix 1 and helix 4
The surface structure reveals two main interaction sites, a shallow <scene name='56/568023/Hydrophobic_pocket/2'>hydrophobic patch</scene> made up of helix 1 and helix 4
which is responsible for the binding of rapamycin  and a <scene name='56/568023/Deep_cleft_helix_2_and_3/8'>deep cleft</scene> between helix 2 and helix 3. This cleft contains
which is responsible for the binding of rapamycin  and a <scene name='56/568023/Deep_cleft_helix_2_and_3/10'>deep cleft</scene> between helix 2 and helix 3. This cleft contains
charged and hydrophobic residues and is expected to function as a binding site for small molecules to regulate
charged and hydrophobic residues and is expected to function as a binding site for small molecules to regulate
mTOR activity.
mTOR activity.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Dimitri Feltrin, Hamelin Baptiste