Conformational Changes in Tyrosine 11 of Neurotensin Are Required to Activate the Neurotensin Receptor 1.

ABSTRACT: Cell-cell communication via endogenous peptides and their receptors is vital for controlling all aspects of human physiology and most peptides signal through G protein-coupled receptors (GPCRs). Disordered peptides bind GPCRs through complex modes for which there are few representative crystal structures. The disordered peptide neurotensin (NT) is a neuromodulator of classical neurotransmitters such as dopamine and glutamate, through activation of neurotensin receptor 1 (NTS₁). While several experimental structures show how NT binds NTS₁, details about the structural dynamics of NT during and after binding NTS₁, or the role of peptide dynamics on receptor activation, remain obscure. Here saturation transfer difference (STD) NMR revealed that the binding mod

SUBMITTER: Bumbak F 

PROVIDER: S-EPMC7432660 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature