Nat. Struct. Biol. 10, 694–700 (2003).
A review by Dwyer and Bradley (cited as ref. 18 in the original article) presented an alignment of the alcohol-sensitive regions of several ion channels and proposed a consensus sequence motif for alcohol-binding sites. Kruse et al. acknowledge that the alignment of Dwyer and Bradley (Fig. 2 of ref. 18) bears superficial similarity to Figure 4 of their paper. Nevertheless, the authors state that the differences between the two are significant. Specifically, Figure 4 of this paper was constructed on the basis of an alignment with the high-resolution structures of LUSH–alcohol complexes. On the basis of this alignment the authors proposed a different consensus motif for alcohol-binding sites. As stated in the manuscript, the authors emphasize that sequence alignments alone are unlikely to define alcohol-binding motifs in these proteins; instead, the conformational proximity of the appropriate amino acids is likely to be more relevant.
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Kruse, S., Zhao, R., Smith, D. et al. Addendum: Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster. Nat Struct Mol Biol 11, 102 (2004). https://doi.org/10.1038/nsmb0104-102b
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DOI: https://doi.org/10.1038/nsmb0104-102b