Disorder transitions and conformational diversity cooperatively modulate biological function in proteins

DIEGO ZEA; ALEXANDER MONZON; CLAUDIA GONZALEZ; MARIA SILVINA FORNASARI; SILVIO TOSATTO; GUSTAVO PARISI

PROTEIN SCIENCE

JOHN WILEY & SONS INC

Año: 2016

0961-8368

Structural differences between conformers sustain protein biological function. Here, westudied in a large dataset of 745 intrinsically disordered proteins, how ordered-disordered transitionsmodulate structural differences between conformers as derived from crystallographic data.We found that almost 50% of the proteins studied show no transitions and have low conformationaldiversity while the rest show transitions and a higher conformational diversity. In this lastsubset, 60% of the proteins become more ordered after ligand binding, while 40% more disordered.As protein conformational diversity is inherently connected with protein function our analysissuggests differences in structure-function relationships related to order-disorder transitions.