Skip to main content
. Author manuscript; available in PMC: 2016 Mar 7.
Published in final edited form as: Biochemistry. 2010 Mar 16;49(10):2279–2287. doi: 10.1021/bi902023y

FIGURE 1.

FIGURE 1

(A) Amino acid alignment of ct-AChBP with other AChBPs and the extracellular domain of nAChR subunits (human α4 and α7). The shortened Cys loop of AChBP is highlighted by asterisks. Residues deemed important for agonist binding are designated with a plus sign; a single black horizontal line lies atop the Cys loop, and a double gray horizontal line lies atop the C loop. The glycosylated Asn122 is designated by an italic letter G, and the caret designates the position of Gln149. The AChBPs listed are ls-AChBP from L. stagnalis, bt-AChBP from B. truncatus, ac-AChBP from A. californica, pf-AChBP from P. fucata, and ct-AChBP from C. teleta. (B) Radial (neighbor-joining) tree based on a Clustal alignment of amino acid sequences of indicated Cys loop receptors. (C) Variation of a conserved amino acid triad found in ct-AChBP. The C loop region from a homology model of ct-AChBP is colored green, Tyr194 brown, Glu203 red, and Gln at position 149 in CPK format.