Since the discovery of intrinsically unstructured/unfolded/disordered proteins (IUPs/IDPs) an answer to the question “how these proteins without spatial active pockets bind to their targets?” has been intensively sought. One school of thought pursued an idea that disorder itself should be the main contributing factor to the target-binding process while another has been identifying transient local secondary structural elements recently named PreSMos (Pre-Structured Motifs) as an important factor for target binding. PreSMos have been observed in ~70% of all IDPs whose structural features have been characterized in detail. To date, the PreSMo concept provides the most convincing structural rationale explaining the IDP-target binding behavior at an atomic resolution. I will present a brief developmental history and common characteristics of PreSMos as well as an updated list of PreSMos with their functional relevance.