Ontology highlight
ABSTRACT:
SUBMITTER: Kruse SW
PROVIDER: S-EPMC4397894 | biostudies-literature | 2003 Sep
REPOSITORIES: biostudies-literature
Kruse Schoen W SW Zhao Rui R Smith Dean P DP Jones David N M DN
Nature structural biology 20030727 9
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 prov ...[more]