PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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