Disorder transitions and conformational diversity cooperatively modulate biological function in proteins

ALEXANDER MIGUEL MONZON; SILVIO TOSATTO; DIEGO JAVIER ZEA; MARÍA SILVINA FORNASARI; GUSTAVO PARISI; CLAUDIA GONZALEZ; SILVIO TOSATTO

PROTEIN SCIENCE

JOHN WILEY & SONS INC

Lugar: New York; Año: 2016

0961-8368

Structural differences between conformers sustain protein biological function. Here, we studied in a large dataset of 745 intrinsically disordered proteins, how ordered-disordered transitions modulate structural differences between conformers as derived from crystallographic data. We found that almost 50% of the proteins studied show no transitions and have low conformational diversity while the rest show transitions and a higher conformational diversity. In this last subset, 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 analysis suggests differences in structure-function relationships related to order-disorder transitions.