Abstract
Binding of Leu-enkephalin and [Rh(III)(η(5)-Cp*)(η(6)-Tyr(1))]Leu-enkephalin to the recently published crystal structures of the μ- and δ-opioid receptor is studied. Docking of free Leu-enkephalin reveals two preferred conformations, one of which suggests an alternative binding site for the tyrosine residue. Furthermore, the three-dimensional solution structure of [Rh(III)(η(5)-Cp*)(η(6)-Tyr(1))]Leu-enkephalin was solved by using 2D NMR spectroscopic techniques.
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