Solution structure of the SH3 domain of phospholipase C-gamma

The 2-dimensional 1H nuclear magnetic resonance analysis of the solution structure of the Src homology 3 (SH3) domain of human phospholipase C-gamma (PLC-gamma) is reported. SH3 domains are key components of intracellular signaling mechanisms, functioning as binding sites for cytoplasmic target proteins. The distinctive features of human PLC-gamma include its eight antiparallel beta strands consisting of two successive Greek-key motifs forming a barrel-like structure, and the aliphatic and aromatic residues forming a hydrophobic pocket on the surface of the molecule.