Wittmann, Hans-Joachim and Strasser, Andrea (2015) Binding pathway of histamine to the hH(4)R, observed by unconstrained molecular dynamics. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 25 (6). pp. 1259-1268. ISSN 0960-894X, 1464-3405
Full text not available from this repository. (Request a copy)Abstract
Histamine binds with high affinity to the human histamine H-4 receptor (hH(4)R). We are the first to examine the complete binding pathway of histamine from the extracellular side to the orthosteric binding site of the hH(4)R by means of unconstrained molecular dynamic simulation. Furthermore, the simulations show that the positively charged amine moiety of the histamine interacts electrostatically with the highly conserved Asp(3.32), while the imidazole moiety forms a hydrogen bond interaction with Glu(5.46) and Gln(7.42). (C) 2015 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEIN-COUPLED RECEPTORS; LIGAND RECOGNITION; SODIUM-IONS; ACTIVATION; MECHANISM; Ligand binding pathway; Histamine H-4 receptor; Histamine; Molecular dynamics |
| Subjects: | 600 Technology > 615 Pharmacy |
| Divisions: | Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 23 Jul 2019 13:03 |
| Last Modified: | 23 Jul 2019 13:03 |
| URI: | https://pred.uni-regensburg.de/id/eprint/5787 |
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