2LYW
Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor
Summary for 2LYW
| Entry DOI | 10.2210/pdb2lyw/pdb |
| Descriptor | Neurotensin receptor type 1, Neurotensin (2 entities in total) |
| Functional Keywords | interaction ligand/receptor, nts1, signaling protein-neuropeptide complex, signaling protein/neuropeptide |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 4856.52 |
| Authors | Monti, J.,Da Costa, G. (deposition date: 2012-09-20, release date: 2012-12-12, Last modification date: 2024-11-06) |
| Primary citation | Da Costa, G.,Bondon, A.,Coutant, J.,Curmi, P.,Monti, J.P. Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor. J.Biomol.Struct.Dyn., 31:1381-1392, 2013 Cited by PubMed Abstract: 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 adaptability of this region; (ii) for bound NT, the extended conformation of its C-terminus is confirmed for the first time in experimental conditions and in the presence of a part of the receptor; and (iii) despite some substitutions, the human receptor residues that are involved in the interaction with NT could be similar to those of the rat receptor which play an important role in NT binding. PubMed: 23140271DOI: 10.1080/07391102.2012.736776 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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