Sandbox Reserved 822
From Proteopedia
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1w1h is the human pleckstrin homology (PH) domain of the 3-phosphoinositide-dependent protein kinase 1 (PDK1), which plays a various role in PI3K signaling pathways. | 1w1h is the human pleckstrin homology (PH) domain of the 3-phosphoinositide-dependent protein kinase 1 (PDK1), which plays a various role in PI3K signaling pathways. | ||
- | PDK1 contains 556 amino acids and phosphorylates and activates at least 24 Proteins of the AGC family of protein kinases. It therefore consists of a N-terminal Ser/Thr kinase catalytic domain (residues 71-359) and the C-terminal pleckstrin homology (PH) domain (residues 459-550). | + | PDK1 contains 556 amino acids and phosphorylates and activates at least 24 Proteins of the AGC (cAMP-dependent, cGMP-dependent, protein kinase C (PKC)) family of protein kinases. It therefore consists of a N-terminal Ser/Thr kinase catalytic domain (residues 71-359) and the C-terminal pleckstrin homology (PH) domain (residues 459-550). |
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. |
Revision as of 01:36, 4 January 2014
This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Description
1w1h is the human pleckstrin homology (PH) domain of the 3-phosphoinositide-dependent protein kinase 1 (PDK1), which plays a various role in PI3K signaling pathways.
PDK1 contains 556 amino acids and phosphorylates and activates at least 24 Proteins of the AGC (cAMP-dependent, cGMP-dependent, protein kinase C (PKC)) family of protein kinases. It therefore consists of a N-terminal Ser/Thr kinase catalytic domain (residues 71-359) and the C-terminal pleckstrin homology (PH) domain (residues 459-550).
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.