Data for: A cryptic symmetry switch allosterically controls how the PF4 self-protein turns into a pathogenic antigen

This dataset contains the original solution Nuclear Magnetic Resonance (NMR) data and Molecular Dynamics (MD) setup and analysis files that support our study of the Platelet Factor 4 (PF4) conformational switch controlling tetramer symmetry. Study Overview: The asymmetry of dimers of dimers formed by PF4 is essential for the exposure of pathogenic neoepitopes in HIT. Our study elucidates the molecular basis of this asymmetry by identifying a cryptic conformational switch that controls the transition from symmetric to asymmetric PF4 tetramers. We demonstrate that mutations targeting this switch (e.g., the L8A mutant) trap PF4 in a symmetric, non-immunogenic conformation (closed-closed topology), markedly reducing its affinity for HIT antibodies. This dataset contains the MD setup and analysis files, as well as the integrated experimental data supporting this allosteric mechanism. Contents of this Dataset Experimental Data: original data files, including NMR chemical shift data for the E1A–T15A, E28A, and K50A alanine-scanning mutants, as well as other related results. MD Simulation Files: the initial and final structures, simulation parameters, and the input files and scripts used for data analysis