The two NK-1 binding sites correspond to distinct, independent, and non-interconvertible receptor conformational states as confirmed by plasmon-waveguide resonance spectroscopy

作者: Isabel D. Alves , Diane Delaroche , Bernard Mouillac , Zdzislaw Salamon , Gordon Tollin

DOI: 10.1021/BI052586D

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摘要: Two nonstoichiometric ligand binding sites have been previously reported for the NK-1 receptor, with use of classical methods (radioligand and second messenger assays). The most populated (major, NK-1M) site binds substance P (SP) is related to adenylyl cyclase pathway. less (minor, NK-1m) P, C-terminal hexa- heptapeptide analogues SP, NK-2 endogenous ligand, neurokinin A, coupled phospholipase C Here, we examined these two plasmon-waveguide resonance (PWR) spectroscopy that allows thermodynamics kinetics ligand−receptor processes accompanying structural changes receptor be monitored, through measurements anisotropic optical properties lipid bilayers into which incorporated. three peptides, propionyl[Met(O2)11]SP(7−11), partially purified has ...

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