Regular ArticleSite-Directed Mutagenesis of the Histamine H1-Receptor Reveals a Selective Interaction of Asparagine207 with Subclasses of H1-Receptor Agonists
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Evolutionary history of histamine receptors: Early vertebrate origin and expansion of the H<inf>3</inf>-H<inf>4</inf> subtypes
2021, Molecular Phylogenetics and EvolutionCitation Excerpt :Interestingly, several predicted sites have pharmacological evidence for their functional roles. For example, Type I residue K1915.40 of human H1 affects agonist and antagonist binding and confers H1 selectivity (Leurs et al., 1995, 1994; ter Laak et al., 1995; Wieland et al., 1999). This site is also responsible for the formation of partial bidentate hydrogen bonding with imidazolyl and similar group containing ligands (Seifert et al., 2013).
Dibenzo[b,f][1,4]oxazepines and dibenzo[b,e]oxepines: Influence of the chlorine substitution pattern on the pharmacology at the H<inf>1</inf>R, H<inf>4</inf>R, 5-HT<inf>2A</inf>R and other selected GPCRs
2016, Pharmacological ResearchCitation Excerpt :Thus, based on the experimental data, it might be suggested that the different positions of one aromatic moiety in the oxazepines and oxepines influence the conformation of the Trp6.48 and determine partial or inverse agonism. Numerous studies were performed to identify amino acids of the TM domains and the extracellular loops at the H1R and H4R, being involved in ligand binding [4,23,47,59–68]. Additionally, at the hH3R and rH3R the amino acids 3.37 and 3.40 were identified to be responsible for species differences [69–71].
Small and colorful stones make beautiful mosaics: Fragment-based chemogenomics
2013, Drug Discovery TodayMolecular and cellular analysis of human histamine receptor subtypes
2013, Trends in Pharmacological SciencesDibasic biphenyl H <inf>3</inf> receptor antagonists: Steric tolerance for a lipophilic side chain
2012, European Journal of Medicinal ChemistryCitation Excerpt :In TM3, the conserved aspartic acid (Asp107) of the H1 crystal structure interacts with the basic nitrogen of doxepin. Asn198 in TM5 of the H1 receptor is thought to bind the imidazole ring of the natural ligand histamine [46], while it does not interact with doxepin in the crystal structure. The corresponding amino acid in the H3 receptor is Glu206, important for histamine and (R)-α-methylhistamine binding, as highlighted by mutagenesis studies [47].
Experimental and quantum-chemical studies of histamine complexes with copper(II) ion
2012, PolyhedronCitation Excerpt :The ligand-binding pockets of each of these receptors were found to contain amino acids that interact with histamine. Examples of such residues are, aspartic acid [18,19], lysine [17,20–22], threonine and phenylalanine [17,19,21]. The endocyclic nitrogen atom of the imidazole ring is believed to be the most preferred site for interactions of histamine with protein receptors.