Sandbox Reserved 825: Difference between revisions

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Helix 3 contains a <scene name='56/568023/Helix_3_bend_residues/3'>bend</scene> of approximately 45° and its N-terminal half is largely disordered.
Helix 3 contains a <scene name='56/568023/Helix_3_bend_residues/3'>bend</scene> of approximately 45° and its N-terminal half is largely disordered.


The surface structure reveals two main interaction sites, a shallow <scene name='56/568023/Hydrophobic_pocket/1'>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_3/8'>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