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Fig. 5 | Biology Direct

Fig. 5

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

Fig. 5

a Residues identified by the PSN-Ensemble program to mediate long-distance interaction between select residues of the BB loop (Pro 434, Gln 432 and Asp 430, blue boxes) and Arg 522 (orange box) in the RK site. It is seen that of the three chosen BB loop residues, the shortest path i.e, the path containing the least number of residues required to mediate interactions, is between Asp 430 and Arg 522. Residues that are common to at least 2 paths of communication are enclosed within coloured boxes. All three paths pass through the residue Phe 437 (red box) as well as residues Ile 399 and Ile 453 (marked within purple box). Residue Leu 439 (green box) and residues Ala 425, Glu 438, Thr 436 (marked within brown box) mediate long-distance communication between Asp 430 and Arg 522 as well as between Pro 434 and Arg 522. b Mapping of the path of communication between the source residues (shown as blue spheres) and sink residue Arg 522(orange spheres) onto the structure of the N-TIR docked complex. (i)Asp 430-Arg 522, (ii) Gln 432-Arg 522 and (iii) Pro 434-Arg 522. The intermediate residues connecting Asp 430 and Arg 522 are shown as pink spheres, those connecting Gln 432 and Arg 522 in light blue spheres while those connecting Pro 434 and Arg 522 are coloured yellow. Residues, that have been marked within the coloured boxes in (a), are highlighted by the same colours on the structure

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