Sandbox Reserved 822: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 41: | Line 41: | ||
=== Interaction with Inositol Phosphates === | === Interaction with Inositol Phosphates === | ||
The structure of the phosphoinositide-binding site of the PDK1 PH domain is unusually spacious. Compared to other PtdIns(3,4,5)P<sub>3</sub>-binding PH domains additional space is present around the D2- and D6-hydroxyl groups, which potentially could accomodate further phosphate groups. This indicates a special affinity of the PDK1 PH domain for inositol phosphates because physiologically they are known to be phosphorylated at the D2 and/or D6 position while phosphoinositides, in contrast, do not show modifications at these positions. | The structure of the phosphoinositide-binding site of the PDK1 PH domain is unusually spacious. Compared to other PtdIns(3,4,5)P<sub>3</sub>-binding PH domains additional space is present around the D2- and D6-hydroxyl groups, which potentially could accomodate further phosphate groups. This indicates a special affinity of the PDK1 PH domain for inositol phosphates because physiologically they are known to be phosphorylated at the D2 and/or D6 position while phosphoinositides, in contrast, do not show modifications at these positions. | ||
In the PDK1 PH domain Ins(1,3,4,5)P<sub>4</sub> complex Ins(1,3,4,5)P<sub>4</sub> interacts with protein side chains only. This results in a significantly reduced number of protein-ligand hydrogen bonds (a total of 11) compared to PH domain Ins(1,3,4,5)P<sub>4</sub> complexes of other proteins which form 15 to 16 hydrogen bonds.<ref name="Structural" /> | In the PDK1 PH domain Ins(1,3,4,5)P<sub>4</sub> complex Ins(1,3,4,5)P<sub>4</sub> interacts with protein side chains only. This results in a significantly reduced number of protein-ligand hydrogen bonds (a total of 11) compared to PH domain Ins(1,3,4,5)P<sub>4</sub> complexes of other proteins which form 15 to 16 hydrogen bonds.<ref name="Structural" /> | ||
