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1ooh
From Proteopedia
Revision as of 14:47, 29 September 2014 by OCA (Talk | contribs)
1ooh is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster.,Kruse SW, Zhao R, Smith DP, Jones DN Nat Struct Biol. 2003 Sep;10(9):694-700. Epub 2003 Jul 27. PMID:12881720[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Kruse SW, Zhao R, Smith DP, Jones DN. Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster. Nat Struct Biol. 2003 Sep;10(9):694-700. Epub 2003 Jul 27. PMID:12881720 doi:10.1038/nsb960
