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. Author manuscript; available in PMC: 2009 Jun 30.
Published in final edited form as: Neuron. 2007 Dec 20;56(6):979–991. doi: 10.1016/j.neuron.2007.11.013

Figure 1. Sequence Conservation within the Neuroligins and Comparison with Human Liver Carboxylesterase and mAChE.

Figure 1

The NL4 sequence displayed is that of the recombinant Gln44-Thr619 protein used for crystallization; the FLAG epitope is not shown. The positions for alternatively spliced inserts A and B are indicated by vertical arrowheads. The NL4 and mAChE numbering and their secondary structure elements are displayed above and below the alignment, respectively. The Cys-loop and loops L1 (α3 6,7-α4 6,7, Thr332-Ile338 in NL4), L2 (α1 7,8-α2 7,8, Asp381-Val390), L3 (β8-α1 8,9, Gln477-Ser487) and L4 (α1 8,9-α2 8,9, Gly503-Ser513) are indicated by gray bars under the alignment. The NL4 residues buried at the Nrxβ1 binding interface are shaded as gray boxes. The mAChE catalytic triad residues are indicated by asterisks; the two NL4 glycosylation sites by triangles; the residue pair involved in Ca2+ binding by filled circles; and the NL3/NL4 residues mutated in autism patients by filled squares. The LRE motif is indicated with a black bar above the sequences.