Structural highlights
Publication Abstract from PubMed
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.
NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition.,Coutant J, Curmi PA, Toma F, Monti JP Biochemistry. 2007 May 15;46(19):5656-63. Epub 2007 Apr 19. PMID:17441729[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coutant J, Curmi PA, Toma F, Monti JP. NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition. Biochemistry. 2007 May 15;46(19):5656-63. Epub 2007 Apr 19. PMID:17441729 doi:10.1021/bi602567p
