Binding pathway of histamine to the hH(4)R, observed by unconstrained molecular dynamics

作者：Wittmann Hans Joachim; Strasser Andrea^*

来源：Bioorganic & Medicinal Chemistry Letters, 2015, 25(6): 1259-1268.

DOI：10.1016/j.bmcl.2015.01.052

• Ligand binding pathway
• Histamine H-4 receptor
• Histamine
• Molecular dynamics

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).

• 出版日期2015-3-15