Disorder transitions and conformational diversity cooperatively modulate biological function in proteins. (18th April 2016)

• Record Type: Journal Article
• Authors: Zea, Diego Javier; Monzon, Alexander Miguel; Gonzalez, Claudia; Fornasari, María Silvina; Tosatto, Silvio C. E.; Parisi, Gustavo
• Is Part Of: Protein science. Volume 25:Number 6(2016:Jun.)
• Page Start: 1138
• Page End: 1146
• Publication Date: 2016-04-18
• Subjects: disorder -- conformational diversity -- protein function -- transitions; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2931
• Languages: English
• ISSNs: 0961-8368

Abstract

Abstract: 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.