Fig. 1From: Integrative modelling of TIR domain-containing adaptor molecule inducing interferon-β (TRIF) provides insights into its autoinhibited stateDomain architecture of TRIF. The full-length TRIF protein is 712 amino acids. The N-terminal protease resistant domain spans residues 1 to 153, residues 154–392 make up the intermediate proline-rich disordered region, residues 393–545 constitute the TIR domain while the C-terminal disordered region comprises of residues 546–712Back to article page