Sandbox Reserved 822: Difference between revisions
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The PH domain of PDK1 possesses an additional extension ('bud') N-terminal to the standard PH domain fold. This bud forms two additional β strands and one α helix and is an integral part of the overall fold. The two β strands β1' and β2'extend the β1 - β4 sheet in an antiparallel fashion through the formation of β sheet hydrogen bonds between β2'and β1. The α helix packs against this newly formed six stranded β sheet forming an additional <scene name='56/568020/Hydrophobic_core/1'>hydrophobic core</scene> outside of the standard PH domain fold. The bud binds to the β1 - β4 sheet by several additional hydrophobic contacts and buries more than 30% of the surface of the standard PH domain fold. | The PH domain of PDK1 possesses an additional extension ('bud') N-terminal to the standard PH domain fold. This bud forms two additional β strands and one α helix and is an integral part of the overall fold. The two β strands β1' and β2'extend the β1 - β4 sheet in an antiparallel fashion through the formation of β sheet hydrogen bonds between β2'and β1. The α helix packs against this newly formed six stranded β sheet forming an additional <scene name='56/568020/Hydrophobic_core/1'>hydrophobic core</scene> outside of the standard PH domain fold. The bud binds to the β1 - β4 sheet by several additional hydrophobic contacts and buries more than 30% of the surface of the standard PH domain fold. | ||
== Ligand Interaction == | |||
The PH domain of PDK1 binds inositol phosphates and phosphatidylinositol phosphates with different affinities depending on the phosphorylation state of the molecules. These interactions target PDK1 to particular locations inside the cell and are therefore crucial for the flawless execution of signaling pathways in which PDK1 is involved. | |||
=== Binding site === | |||
