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NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition.

Coutant J, Curmi PA, Toma F, Monti JP

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.

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.

Published 9 May 2007 in Biochemistry, 46(19): 5656-63.
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