2lyw | pdb_00002lyw

Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor

spinqualitylabelsall models 2lyw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lyw is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NTR1_HUMAN Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. Publication Abstract from PubMed 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. Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor.,Da Costa G, Bondon A, Coutant J, Curmi P, Monti JP J Biomol Struct Dyn. 2012 Nov 12. PMID:23140271 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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