PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15306657-2	2004	To determine the binding site for a competitive inverse agonist, midazolam, three of the four residues that directly contact TRH and other residues that restrain TRH-R1 in an inactive conformation were screened by mutagenesis and binding assays.	Midazolam	65-74	thyrotropin releasing hormone	Homo sapiens	125-128	
15306657-2	2004	To determine the binding site for a competitive inverse agonist, midazolam, three of the four residues that directly contact TRH and other residues that restrain TRH-R1 in an inactive conformation were screened by mutagenesis and binding assays.	Midazolam	65-74	thyrotropin releasing hormone	Homo sapiens	162-165	
15306657-3	2004	We found that two residues that directly contact TRH, Asn-110 in transmembrane helix 3 (3.37) and Arg-306 in transmembrane helix 7 (7.39), were important for midazolam binding but another, Tyr-282 in transmembrane helix 6 (6.51), was not.	Midazolam	158-167	thyrotropin releasing hormone	Homo sapiens	49-52	
15306657-4	2004	A highly conserved residue, Trp-279 in transmembrane helix 6 (6.48), which was reported to be critical in stabilizing TRH-R1 in an inactive state but not for TRH binding, was critical for midazolam binding.	Midazolam	188-197	thyrotropin releasing hormone	Homo sapiens	118-121	
15306657-5	2004	We used our previous model of the unoccupied TRH-R1 to generate a model of the TRH-R1/midazolam complex.	Midazolam	86-95	thyrotropin releasing hormone	Homo sapiens	45-48	
15306657-5	2004	We used our previous model of the unoccupied TRH-R1 to generate a model of the TRH-R1/midazolam complex.	Midazolam	86-95	thyrotropin releasing hormone	Homo sapiens	79-82	
15306657-6	2004	The experimental results and the molecular model of the complex suggest that midazolam binds to TRH-R1 within a transmembrane helical pocket that partially overlaps the TRH binding pocket.	Midazolam	77-86	thyrotropin releasing hormone	Homo sapiens	96-99	
15306657-6	2004	The experimental results and the molecular model of the complex suggest that midazolam binds to TRH-R1 within a transmembrane helical pocket that partially overlaps the TRH binding pocket.	Midazolam	77-86	thyrotropin releasing hormone	Homo sapiens	169-172	
15306657-8	2004	We suggest that the mechanism of inverse agonism effected by midazolam involves its direct interaction with Trp-279, which contributes to the stabilization of the inactive conformation of TRH-R1.	Midazolam	61-70	thyrotropin releasing hormone	Homo sapiens	188-191