title: Determinants of histamine recognition: implications for the design of antihistamines.
abstract: Towards understanding how histamine, a vital neurotransmitter, can perform multiple physiological tasks, an analysis of the different proteins that bind histamine is reported here. Their structural comparison reveals conformational rigidity of histamine. Yet, flexibility in the modes of histamine binding has been observed, which appears to suit specific biological roles of the proteins. These results will be helpful in developing specific antihistamines and also in understanding the pharmacological and toxicological profiles of existing antihistamines.
authors.affiliation: Bioinformatics Centre, Indian Institute of Science, Bangalore 560 012, India.
authors.forename: V Badireenath
authors.initials: VB
authors.lastname: Konkimalla
authors.forename: Nagasuma
authors.initials: N
authors.lastname: Chandra
mesh_terms: D000936:Antigen-Antibody Complex / Q000737:chemistry; D001665:Binding Sites; D003198:Computer Simulation; D030562:Databases, Protein; D015195:Drug Design; D004798:Enzymes / Q000737:chemistry; D006632:Histamine / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D018494:Histamine Agents / Q000737:chemistry; D006634:Histamine H1 Antagonists / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D046911:Macromolecular Substances; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D011968:Receptors, Histamine / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D000936:Antigen-Antibody Complex; D004798:Enzymes; D018494:Histamine Agents; D006634:Histamine H1 Antagonists; D046911:Macromolecular Substances; D011968:Receptors, Histamine; D006632:Histamine