Extended Data Fig. 5: Meta-stable state MS1 exhibits conformational features consistent with DM susceptibility.
From: MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange
a Significant (2-σ) conformational differences between MS1 (blue ribbons) and MS3 (white ribbons) both sampled uniformly from all simulated allotypes are highlighted by magenta arrows in a superposition of representative MS conformations. b. Significant polar interaction frequency differences as derived by PySFD28 between MS1 and MS3 are mapped as blue bars onto a representative conformation of MS3, shown in white ribbons (the CLIP peptide is shown in green). These bars form a network of interaction changes that span the entire DM interaction interface on MHCII. Residues, for which it is known from the literature6,29 that mutations affect DM-susceptibility, locate to the same region (α40, 43, 49, 51, 53, 54, 55, 57, 61, 96, 100 and β84, 87, 152, 184, 187 shown as cyan spheres) except for three residues (α100 and β184, 187 shown as yellow spheres). Residues, where mutations are known not to affect DM-susceptibility are shown as red spheres (α62, 69, 76, 81) and are outside the network.
