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![[Figure 4]](gi5034fig4mag.jpg)
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Figure 4
(a) Alignment of selected sequence segments that form the orthosteric binding sites in AcAChBP and α4, α7 and β2 nAChRs. Loops are labelled and are split into principal (+) and complementary (−) sides. Residues coloured blue are key and are discussed in the text. Val125 and Thr127 of AcAChBP are in the N-terminal section of loop E but are left out for clarity. (b) A schematic of the orthosteric binding site listing the key residues of AcAChBP and the corresponding residues in the α4(+)β2(−) nAChR heteromeric site. Loop F is out of range of the ligands discussed in this work and has been omitted. Arg96 is included given its role in binding the anion (see text). Boxes are coloured yellow to highlight strict conservation, grey for the (+) side and cyan for the (−) side. (c) Schematic with the same format for the α7 nAChR homomeric site. |
![[Figure 4]](gi5034fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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