TY - DATA T1 - WT CD28 can adopt a stable conformation that would allow bivalent binding. PY - 2014/02/24 AU - Mariano Sanchez-Lockhart AU - Ana V. Rojas AU - Margaret M. Fettis AU - Richard Bauserman AU - Trissha R. Higa AU - Hongyu Miao AU - Richard E. Waugh AU - Jim Miller UR - https://plos.figshare.com/articles/figure/_WT_CD28_can_adopt_a_stable_conformation_that_would_allow_bivalent_binding_/943320 DO - 10.1371/journal.pone.0089263.g006 L4 - https://ndownloader.figshare.com/files/1397021 KW - Biochemistry KW - proteins KW - Immune system proteins KW - Protein interactions KW - protein structure KW - T-cell receptors KW - Transmembrane proteins KW - Biomacromolecule-ligand interactions KW - Macromolecular assemblies KW - biophysics KW - immunology KW - Immune cells KW - t cells KW - Immune response KW - immunomodulation KW - Molecular cell biology KW - Signal transduction KW - Mechanisms of signal transduction KW - crosstalk KW - Membrane receptor signaling KW - Immunologic receptor signaling KW - Signaling in cellular processes KW - Transmembrane signaling KW - cell adhesion KW - Computer modeling KW - Computerized simulations KW - cd28 KW - conformation KW - bivalent N2 - MD simulations were run with WT CD28 starting from a rotated dimer orientation predicted from the simulations starting from the CTLA-4 dimer orientation. (A) The RMSD with respect to the initial conformation for three independent trajectories indicate that these dimer conformers are very stable. (B) When CD80 molecules were docked onto the conformations, there was no surface buried between the ligands, indicating that all conformations were bivalent. A representative bivalent conformation of CD28 (green) with docked CD80 molecules (cyan) is shown to illustrate the CD28 dimer (C) and in a rotated view to show the orientation of the docked CD80 molecules (D). ER -