Prediction of protein-protein interfaces on G-protein beta subunits reveals a novel phospholipase C beta2 binding domain.

ABSTRACT: Gbeta subunits from heterotrimeric G-proteins (guanine nucleotide-binding proteins) directly bind diverse proteins, including effectors and regulators, to modulate a wide array of signaling cascades. These numerous interactions constrained the evolution of the molecular surface of Gbeta. Although mammals contain five Gbeta genes comprising two classes (Gbeta1-like and Gbeta5-like), plants and fungi have a single ortholog, and organisms such as Caenorhabditis elegans and Drosophila melanogaster contain one copy from each class. A limited number of crystal structures of complexes containing Gbeta subunits and complementary biochemical data highlight specific sites within Gbetas needed for protein interactions. It is difficult to determine from these interaction sites what, if any, additional

SUBMITTER: Friedman EJ 

PROVIDER: S-EPMC2767172 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature