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. 2018 Jan 29;9:75. doi: 10.3389/fimmu.2018.00075

Figure 1.

Figure 1

Overall topology of the toll/interleukin 1 receptor (TIR) domain-containing adaptor protein (TIRAP). (A) The overall domain organization of TIRAP. Amino acid positions are indicated at the bottom of each segment. (B) The predicted secondary structure of residues 1−120 showing the random coiled nature of the N-terminal domain (NTD; residues 1−83). The phosphatidylinositol (PI)-binding motif (PBM; residues 15−35) and the PI-binding domain (PBD; residues 1−40) are enclosed in teal and black boxes, respectively. (C) A three-dimensional model of the NTD (residues 1−78) showing the PI-binding residues: K15 and K16 at one end and K31 and K32 at the other end of the α helix (residues 17−31). Although NTD spans residues 1–83, we modeled only residues 1–78, as residues 79–221 are present in the crystal structure of the TIR domain (PDB ID: 3UB2). (D) The NMR-derived structure of PBM (PDB ID: 5T7Q; residues 15−35).