Does functional coupling promote high-affinity agonist binding to Neurotensin receptor NTS-1?
BMC Cancer 11, 421 (2011). Grisshammer, R. & Hermans, E. Functional coupling with Galpha (q) and Galpha (i1) protein subunits promotes high-affinity agonist binding to the neurotensin receptor NTS-1 expressed in Escherichia coli.
Does ml314 bias NTS 1 pharmacology?
Taken together, we hypothesize that ML314, and its successor SBI-553 72, 73, may bias NTS 1 pharmacology by stabilizing signaling incompetent G protein conformations, such as a non-canonical Gα subunit 24, 25 and/or α5-helix pose 74, 75.
What is a PIP2 molecule in a NTS 1 ARR1 cryo-EM complex?
A NTS 1 :βArr1 cryo-EM complex includes one PIP2 molecule bound in a pocket formed by the intracellular portions of TMs 1/2/4 23; comparison with both canonical and non-canonical NTS 1 :G protein cryo-EM models suggests this PIP2 position could also coordinate the interaction of NTS 1 with the Gαβ subunits 24, 25.
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