Skip to main content


Fig. 4 | Biology Direct

Fig. 4

From: Integrative modelling of TIR domain-containing adaptor molecule inducing interferon-β (TRIF) provides insights into its autoinhibited state

Fig. 4

a Zoom-in of the interface showing hydrophobic interactions, with the residues of interest being represented as sticks. The residues Phe 12 and Trp 77 on the N-terminal domain (purple) are located in close proximity to Phe 431 of the TIR domain (green). b A plot of minimum distance between select residue pairs: Leu 108-Phe 431(black), Ile 14-Phe 431(red), Leu 51-Phe 431(green),Phe 12-Phe 431 (blue) and Trp 77-Phe 431(yellow) throughout the time course of the simulation. Phe431 of the TIR domain appears to play an important role in the interaction of the domains. c Residues involved in the formation of stable inter-domain hydrogen bonds. The residues Gln 20, Asp 21, Lys 22 of the N-terminal domain (purple) and residues Gln 443, Gln 471 of the TIR domain (green) are represented as sticks. d Percent hydrogen bond occupancy between the different donor-acceptor residue pairs as shown in c

Back to article page