PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12660235-5 2003 A structural model of the ligand-binding domain of the 5-HT3R based on the acetylcholine binding protein revealed the position of the mutated amino acids. Acetylcholine 75-88 5-hydroxytryptamine receptor 3A Homo sapiens 55-61 15318223-3 2004 Here we identify structural requirements for functionally coupling the two domains by combining acetylcholine (ACh)-binding protein, whose structure was determined at atomic resolution, with the pore domain from the serotonin type-3A (5-HT3A) receptor. Acetylcholine 96-109 5-hydroxytryptamine receptor 3A Homo sapiens 235-241 15318223-4 2004 Only when amino-acid sequences of three loops in ACh-binding protein are changed to their 5-HT3A counterparts does ACh bind with low affinity characteristic of activatable receptors, and trigger opening of the ion pore. Acetylcholine 49-52 5-hydroxytryptamine receptor 3A Homo sapiens 90-96