Sandbox Reserved 822: Difference between revisions
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PDK1 is activated by binding of its PH domain to specific target molecules like phosphoinositides or phosphoatityl inositides and can then interact with its target substrates. | PDK1 is activated by binding of its PH domain to specific target molecules like phosphoinositides or phosphoatityl inositides and can then interact with its target substrates. | ||
Even though the targeting of PDK1 to specific locations of the cell is not fully understand in detail, it has been proven that the binding of its PH domain to target molecules plays a central role in this process.<ref name="Structural"> PMID: | Even though the targeting of PDK1 to specific locations of the cell is not fully understand in detail, it has been proven that the binding of its PH domain to target molecules plays a central role in this process.<ref name="Structural"> PMID: 15457207 </ref> | ||
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The PH domain of PDK1 reveals a structural variation of a standard PH domain fold with an additional 'bud' at the N-terminus. | The PH domain of PDK1 reveals a structural variation of a standard PH domain fold with an additional 'bud' at the N-terminus. | ||
[[Image:Topology_Diagram_of_PH_domain_of_PDK1.JPG|left|320px|thumb|Fig.1 Topology diagram of the PH domain of PDK1. The colors of the different sections correspond to the coloring of the Jmol structure applet. <ref name="Structural"> PMID: | [[Image:Topology_Diagram_of_PH_domain_of_PDK1.JPG|left|320px|thumb|Fig.1 Topology diagram of the PH domain of PDK1. The colors of the different sections correspond to the coloring of the Jmol structure applet. <ref name="Structural"> PMID: 15457207 </ref>]] | ||
The standard PH domain fold consists of mainly three different sections: | The standard PH domain fold consists of mainly three different sections: | ||
