Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor.

@article{Costa2013IntermolecularIB,
  title={Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor.},
  author={Gr{\'e}gory da Costa and Arnaud Bondon and J{\'e}r{\^o}me Coutant and Patrick A. Curmi and J. C. Monti},
  journal={Journal of biomolecular structure & dynamics},
  year={2013},
  volume={31 12},
  pages={1381-92}
}
Neurotensin (NT) is a tridecapeptide hormone in the periphery and neurotransmitter in the brain that principally activates three receptor subtypes, named NTS1, NTS2, and NTS3. Since little is known about its structure in the presence of its principal receptor NTS1, we determined it using the key domain of the receptor, i.e. the third extracellular loop. We conclude the following: (i) for the receptor fragment, NT binding modifies its central part, underlying the great flexibility and… CONTINUE READING

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