Structure of the extracellular domain of TDR and TDIF complex.

<p>(A) Top view of the TDR-TDIF structure in cartoon representation with smoothed loops. The disordered region in TDR structure (residues 48–56) is drawn in dotted line. Five glycosylated asparagine residues and the four cysteine residue that form two disulfide bonds between four neighboring leucine-rich repeats of TDR are depicted in stick representation and colored in orange and red, respectively. The structure of the TDR structure is shown in cyan, and the TDIF peptide structure is colored in red. The LRR repeat numbers are indicated on the structure. (Negatively charged surface is shown in red, and positively charged surface is depicted in blue). (B) Side view of the TDR-TDIF structure showing the superhelical S shaped structure. (C) Surface representation of the TDR-TDIF complex structure; positively charged surface is depicted in blue, and negatively charged surface is colored in red. (D) The TDIF peptide structure enveloped in a f_o-f_c difference map contoured in 3 δ.