title: Disorder transitions and conformational diversity cooperatively modulate biological function in proteins.
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.
authors.affiliation: Structural Bioinformatics Group, Department of Science and Technology, National University of Quilmes, Argentina.
authors.forename: Diego Javier
authors.initials: DJ
authors.lastname: Zea
authors.affiliation: Structural Bioinformatics Group, Department of Science and Technology, National University of Quilmes, Argentina.
authors.forename: Alexander Miguel
authors.initials: AM
authors.lastname: Monzon
authors.affiliation: Structural Bioinformatics Group, Department of Science and Technology, National University of Quilmes, Argentina.
authors.forename: Claudia
authors.initials: C
authors.lastname: Gonzalez
authors.affiliation: Structural Bioinformatics Group, Department of Science and Technology, National University of Quilmes, Argentina.
authors.forename: María Silvina
authors.initials: MS
authors.lastname: Fornasari
authors.affiliation: Biocomputing up, Department of Biomedical Sciences, University of Padova, Italy.
authors.forename: Silvio C E
authors.initials: SC
authors.lastname: Tosatto
authors.affiliation: Structural Bioinformatics Group, Department of Science and Technology, National University of Quilmes, Argentina.
authors.forename: Gustavo
authors.initials: G
authors.lastname: Parisi
mesh_terms: D030562:Databases, Protein; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics*; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: conformational diversity; disorder; protein function; transitions