Structural biology and drug design: conformational stability, flexibility and disordering; the SARS-CoV-1/SARS-CoV-2 main protease; first two Springer/IUCr Briefs

Abstract

Proteins perform incredibly diverse and highly selective functions. It is the consequence of their finely tuned three-dimensional structure. The ‘lock-and-key’ model used for more than a century refers to the classical structure-function paradigm. However, as Professor Giuseppe Zanotti of theUniversity of Padua, Italy reviews for usmany protein functions do not require a unique structure. The carriers of such structure-independent functions are the intrinsically disordered regions among ordered domains of proteins (IDRs), or the fully, intrinsically, disordered proteins (IDPs). IDRs and IDPs frequently occur in nature in all proteomes of organisms. The abundance of disorder, the lack of a fixed quaternary protein structure increases proportionally with the complexity of the organism. The presence of significantly disordered regions is estimated around 33% in the eukaryotic proteins and 35% in the human proteome. And in his final note, Giuseppe Zanotti states