glutamate (E200) and arginine (R209) participate in binding of cAMP, which causes a conformational change in the loop that prevents binding of the loop to the C subunit.

TLS Online TPP Program

#Id: 9671

#XL - T Zoology

PH domain of PKB binds with high affinity to the 

3-phosphates in both PI(3,4)P2 and PI(3,4,5)P3

TLS Online TPP Program

#Id: 9672

#XL - T Zoology

In unstimulated cells, 

concentration of phosphoinositides is low, and PKB is

inactive because its PH domain physically blocks the kinase active site

TLS Online TPP Program

#Id: 9673

#XL - T Zoology

Ligand-induced receptor activation,

Concentration of PI 3-phosphates rises

PH domain of PKB binds to PI 3-phosphates

TLS Online TPP Program

#Id: 9674

#XL - T Zoology

Maximal activation of PKB depends on recruitment to the cytosolic surface of the plasma membrane of two other kinases -PDK1 and PDK2.

TLS Online TPP Program

#Id: 9675

#XL - T Zoology

PDK1 can phosphorylate PKB on a critical threonine residue in its activation loop

TLS Online TPP Program

#Id: 9676

#XL - T Zoology

Phosphorylation by the mTORC2 kinase complex, of a second serine on

PKB that is not in the activation loop is necessary for maximal PKB activity