title: NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition.
abstract: Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple biological functions in the central and peripheral nervous system. Little is known about the structure of this neuropeptide, and what is known only concerns its C-terminal part. We determined here for the first time the structure of the full-length NT in membrane-mimicking environments by means of classical proton-proton distance constraints derived from solution-state NMR spectroscopy. NT was found to have a structure at both its N and C termini, whereas the central region of NT remains highly flexible. In TFE and HFIP solutions, the NT C-terminus presents an extended slightly incurved structure, whereas in DPC it has a beta turn. The N-terminal region of NT possesses great adaptability and accessibility to the microenvironment in the three media studied. Altogether, our work demonstrates a structure of NT fully compatible with its NTR-bound state.
authors: Laboratoire de Physique et Biophysique GESVAB EA 3675, Institut des Sciences de la Vigne et du Vin, Université de Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France.
authors: Jérome
authors: J
authors: Coutant
authors: Patrick A
authors: PA
authors: Curmi
authors: Flavio
authors: F
authors: Toma
authors: Jean-Pierre
authors: JP
authors: Monti
mesh_terms: D008958:Models, Molecular; D009496:Neurotensin / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D018028:Receptors, Neurotensin / Q000378:metabolism*
chemical_list: D018028:Receptors, Neurotensin; D009496:Neurotensin