The adaptator proteins play an important role in many transduction pathways
by coupling directly or not transmembrane receptors. They are composed of
several domains, the most common being SH2, PTB, PH, SH3 and WW. These doma
ins are found in many signal transduction proteins because they allow speci
fic protein-protein recognition. The SH2 and PTB domains recognize tyrosine
phosphorylated peptides whereas SH3 and WW domain specifically bind to pro
line rich peptides in the type helical polyproline conformation. The presen
t review aims at presenting a structural biology point of view of some of t
he domains involved in adaptors and the role of the three dimensional assem
bly of these domains to gain functionality.