Structural homology model of hTAAR5 with highlighted amino acid positions that were substituted to design chimeric human-murine receptors.

<p>The design of a structural homology model of hTAAR5 was already reported [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0117774#pone.0117774.ref043" target="_blank">43</a>]. We used this 3D information to visualize the amino acids differing between human and mice TAAR5 in accordance to observed differences in the sequence of both species (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0117774#pone.0117774.g004" target="_blank">Fig. 4</a>) with a focus on residues that are in spatial proximity to the extracellular ligand binding part or the intracellular effector binding region. The human wild type amino acids (shown by atom spheres) and the equivalent residues in mouse are provided as mutations in the labels. H1–7 = seven-transmembrane helices 1–7; H8 = eighth intracellular helix; ECL = extracellular loop, ICL = intracellular loop, Ntt = N-terminal tail; Ctt = C-terminal tail.