Structural And Functional Characterization Of An Unusual Sh3 Domain From The Fungal Adaptor Protein Bem1

Protein interactions form the basis of most biological processes and in eukaryotes are often mediated by conserved modular domains that recognize linear motifs. Among the most common protein interaction domains is the SH3 domain that generally recognizes PxxP containing peptides. SH3 domains are approximately 60 amino acids long and are composed of five beta strands. We are studying the SH3 domain from the fungal adaptor protein Bem1p that plays an important role during polarized growth and activation of MAPK signaling pathways.