3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase.

ABSTRACT: New developments regarding the structure and in vivo dynamics of protein kinase B (PKB/Akt) have been recently exposed. Here, we specifically review how the use of multi-disciplinary approaches has resulted in reaching the recent progress made to relate the quaternary structure of PKB to its in vivo function. Using X-ray crystallography, the structure of PKB pleckstrin homology (PH) and kinase domains was determined separately. The molecular mechanisms involved in (a) the binding of the phosphoinositides to the PH domain and (b) the activation of the kinase with the rearrangement of the catalytic site and substrate binding were determined. In vitro, nuclear magnetic resonance and circular dychroism studies gave complementary information on the interaction of the PH domain with the phosphoi

SUBMITTER: Calleja V 

PROVIDER: S-EPMC2682354 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature