Title : Ligand-induced disorder-to-order transitions characterized by structural proteomics and molecular dynamics simulations.

Pub. Date : 2020 Jan 16

PMID : 31683063






1 Functional Relationships(s)
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1 We show here that both an ATP-independent protein chaperone, Spy L32P, and the FK506 binding domain of a prolyl isomerase, FKBP-25 F145A/I223P, are disordered, yet exhibit structures that are distinct from chemically denatured unfolded states in solution, and that they undergo transitions to a more structured state upon ligand binding. Adenosine Triphosphate FKBP prolyl isomerase 3 Homo sapiens