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Pin1 is a modular peptidyl-prolyl isomerase specific for phosphorylated Ser/Thr-Pro (pS/T-P) motifs, typically within intrinsically disordered regions of signaling proteins. Pin1 consists of two flexibly linked domains: an N-terminal WW domain for substrate binding and a larger C-terminal peptidyl-prolyl isomerase (PPIase) domain. Previous studies showed that binding of phosphopeptide substrates to...
We describe a method that uses direct 13 C-detection for measuring rotating-frame carbonyl ( 13 CO) relaxation rates to describe protein functional dynamics. Key advantages of method include the following: (i) unique access to 13 CO groups that lack a scalar-coupled 15 N– 1 H group; (ii) insensitivity to 15 N/ 1 H exchange-broadening that can...
Pin1 is a peptidyl-prolyl isomerase consisting of a WW domain and a catalytic isomerase (PPIase) domain connected by a flexible linker. Pin1 recognizes phospho-Ser/Thr-Pro motifs in cell-signaling proteins, and is both a cancer and an Alzheimer's disease target. Here, we provide novel insight into the functional motions underlying Pin1 substrate interaction using nuclear magnetic resonance deuterium...
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