2OYV
Neurotensin in DPC micelles
Summary for 2OYV
| Entry DOI | 10.2210/pdb2oyv/pdb |
| Related | 2OYW |
| NMR Information | BMRB: 15145 |
| Descriptor | neurotensin (1 entity in total) |
| Functional Keywords | type i turn, neuropeptide |
| Total number of polymer chains | 1 |
| Total formula weight | 1675.95 |
| Authors | Monti, J.P.,Coutant, J.,Curmi, P.A. (deposition date: 2007-02-23, release date: 2007-05-08, Last modification date: 2024-10-30) |
| Primary citation | Coutant, J.,Curmi, P.A.,Toma, F.,Monti, J.P. NMR Solution Structure of Neurotensin in Membrane-Mimetic Environments: Molecular Basis for Neurotensin Receptor Recognition. Biochemistry, 46:5656-5663, 2007 Cited by PubMed 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. PubMed: 17441729DOI: 10.1021/bi602567p PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
