Fig. 1.
Homotypic interaction of TICAM-1 and TICAM-2 TIR domains. (A) TIR domains of TICAM-1 and TICAM-2. The gray boxes represent the TIR domains of TICAM-1 and TICAM-2. (B) Sequence alignment of the TIR domains of human TICAM-1 and human TICAM-2. Amino acid residues involved in the β-sheet and α-helix are shown in blue and red, respectively. The residues on the BB-loop enclosed by a red line were substituted by His for the solution structure determination in this study. Numbers at the right side of the sequences correspond to the residue number in human TICAM-1 and TICAM-2. (C) Yeast two-hybrid analysis of homotypic interaction in TICAM-1 and TICAM-2. Pro434 of TICAM-1, Pro116 and Cys117 of TICAM-2 in the BB-loop were substituted by His residue. These mutants disrupted homotypic interaction of the TIR domain in TICAM-1 and TICAM-2. p53/T-antigen and Lamine/T-antigen were used as positive and negative controls in the yeast two-hybrid assay, respectively. SD-LW, SD-LWH, and SD-LWHA indicate a synthetic dropout medium lacking Leu and Trp, lacking Leu, Trp, and His, and that further lacking Ade, respectively.