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 :This site is conserved in H1 and divergent in H4 (Table S8). Among Type II sites, residues N1985.461 of H1 (Leurs et al., 1994; Moguilevsky et al., 1995; Ohta et al., 1994) and E2065.461 in human H3 (Uveges et al., 2002) and E1825.461 in human H4 (Kiss et al., 2008; Shin et al., 2002) are known to affect histamine binding and determine subtype selectivity (Seifert et al., 2013). The list of predicted sites for which putative functional roles are supported by biochemical evidence is given (Table S10).
Small and colorful stones make beautiful mosaics: Fragment-based chemogenomics
2013, Drug Discovery TodayCitation Excerpt :This also explains the relatively low log(P) values of H3R and H4R ligands (Fig. 2a). H1R also contains D3.32 [46,47], but possesses a neutral N5.46 residue [47,48] (instead of the negatively charged E5.46 in H3R and H4R) as well as an aromatic cluster of phenylalanines (F4326.52/F4356.55) [47,49] which is not present in H3R (T3756.52/M3786.55) and H4R (S3206.52/T3236.55) [27,50], as illustrated in Fig. 3c,d. The requirements of the H1R binding pocket [23] match H1R fragment hits which contain a positively ionizable group and few non-ionizable H-bond donors (Fig. 2a) in combination with rigid aromatic ring structures (data not shown).
Molecular 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 ChemistryExperimental and quantum-chemical studies of histamine complexes with copper(II) ion
2012, PolyhedronCitation Excerpt :The formation of the Cu(II)–histamine complexes could have an effect on the interaction of metal with proteins in the enzymatic reactions. Therefore, histamine coordination through Cu(II) is considered to represent a model system for metal–enzyme studies [18–22,26]. Formation of mixed-ligand complexes of Cu(II), Co(II) and Ni(II) with histamine and diacetyl monooxime [40] as well as with histamine and ATP or UTD [41] was investigated.