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Nat Struct Biol. 2003 Sep;10(9):694-700. Epub 2003 Jul 27.

Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster.

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1
Department of Pharmacology, University of Colorado Health Sciences Center, M/S C236, 4200 East Ninth Avenue, Denver, Colorado 80262, USA.

Erratum in

  • Nat Struct Biol. 2004 Jan;11(1):102.

Abstract

We have solved the high-resolution crystal structures of the Drosophila melanogaster alcohol-binding protein LUSH in complex with a series of short-chain n-alcohols. LUSH is the first known nonenzyme protein with a defined in vivo alcohol-binding function. The structure of LUSH reveals a set of molecular interactions that define a specific alcohol-binding site. A group of amino acids, Thr57, Ser52 and Thr48, form a network of concerted hydrogen bonds between the protein and the alcohol that provides a structural motif to increase alcohol-binding affinity at this site. This motif seems to be conserved in a number of mammalian ligand-gated ion channels that are directly implicated in the pharmacological effects of alcohol. Further, these sequences are found in regions of ion channels that are known to confer alcohol sensitivity. We suggest that the alcohol-binding site in LUSH represents a general model for alcohol-binding sites in proteins.

PMID:
12881720
PMCID:
PMC4397894
DOI:
10.1038/nsb960
[Indexed for MEDLINE]
Free PMC Article
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