ACTIVATING PK B/AKT
J. Yang et al., "Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation," Molecular Cell, 9:1227-40, 2002.
"This contribution is important because it presents the crystal structure of the catalytic domain of Akt/protein kinase B and presents a molecular explanation for why phosphorylation of the hydrophobic motif stabilizes the conformation of AGC kinases. Specifically, the authors propose that phosphorylation of the hydrophobic motif orders the C helix to more favorably align residues for catalysis."
--Alexandra Newton,
University of California, San Diego, US
ASSEMBLING POROUS SOLIDS
C.J. Kuehl et al., "Coordination-driven self assembly: solids with bidirectional porosity," Journal of the American Chemical Society, 124:7266-7, June 26, 2002.
"The authors show that a very large dipyridyl macrocycle self-assembles with Pt(II) ions to form a highly porous crystalline solid containing two types of channels perpendicular to one another. There is continuing interest in designing synthetic zeolites ...
