Different antagonist binding properties of human and rat histamine H3 receptors.
Different histamine H3-receptor antagonists have been tested in displacement studies at human and rat H3 receptors in stably transfected cells. Based on an actual rhodopsin structure, models for receptor antagonist interaction were developed for receptors of both species. Similarities and discrepancies in binding profiles can be explained, but not quantified by hydrophilic interactions with Asp114 and an important lipophilic binding pocket modified by two nearby amino acids.
Stark
H
H
Freie Universität Berlin, Institut für Pharmazie, Berlin, Germany. h.stark@pharmchem.uni-frankfurt.de
Sippl
W
W
Ligneau
X
X
Arrang
J M
JM
Ganellin
C R
CR
Schwartz
J C
JC
Schunack
W
W
D000818:Animals; D016466:CHO Cells / Q000378:metabolism; D006224:Cricetinae; D005260:Female; D006633:Histamine Antagonists / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D007093:Imidazoles / Q000737:chemistry* / Q000494:pharmacology; D008958:Models, Molecular; D011485:Protein Binding; D051381:Rats; D018100:Receptors, Histamine H3 / Q000737:chemistry* / Q000187:drug effects*; D012243:Rhodopsin / Q000737:chemistry; D013045:Species Specificity
D006633:Histamine Antagonists; D007093:Imidazoles; D018100:Receptors, Histamine H3; C115705:ciproxifan; D012243:Rhodopsin