Ontology highlight
ABSTRACT:
SUBMITTER: Nemecz A
PROVIDER: S-EPMC3234955 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20111018 49
Determining the structure of the ligand-binding domain of the nicotinic acetylcholine receptor (nAChR) has been a long standing goal in the design of selective drugs useful in implicated diseases for this prevalent receptor family. Acetylcholine-binding proteins have proven to be valuable surrogates with structural similarity and sequence identity to the extracellular domain of the nicotinic receptor, yet these soluble proteins have their unique features and do not serve as exact replicates of t ...[more]