Another twist in helix C and a missing pocket.
PKB/Akt reveals a major role for helix C in the regulation of activity in the first structure of an AGC family protein kinase in its low-activity form.
Goldsmith
Elizabeth J
EJ
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, 75390, USA.
Chang
Chung-I
CI
D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry*; D017869:Cyclic GMP-Dependent Protein Kinases / Q000737:chemistry*; D008958:Models, Molecular; D011493:Protein Kinase C / Q000737:chemistry*; D017346:Protein Serine-Threonine Kinases; D017433:Protein Structure, Secondary; D011518:Proto-Oncogene Proteins / Q000737:chemistry*; D051057:Proto-Oncogene Proteins c-akt
D011518:Proto-Oncogene Proteins; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt; D017868:Cyclic AMP-Dependent Protein Kinases; D017869:Cyclic GMP-Dependent Protein Kinases; D011493:Protein Kinase C