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Binding pathway of histamine to the hH4R, observed by unconstrained molecular dynamics

Wittmann, Hans-Joachim and Strasser, Andrea (2015) Binding pathway of histamine to the hH4R, observed by unconstrained molecular dynamics. Bioorganic & Medicinal Chemistry Letters 25, pp. 1259-1268.

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Abstract

Histamine binds with high affinity to the human histamine H4 receptor (hH4R). We are the first to examine the complete binding pathway of histamine from the extracellular side to the orthosteric binding site of the hH4R by means of unconstrained molecular dynamic simulation. Furthermore, the simulations show that the positively charged amine moiety of the histamine interacts electrostatically ...

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Item type:Article
Date:2015
Institutions:Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer)
Identification Number:
ValueType
10.1016/j.bmcl.2015.01.052DOI
Keywords:igand binding pathway; Histamine H4 receptor; Histamine; Molecular dynamics
Dewey Decimal Classification:600 Technology > 615 Pharmacy
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:31424
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