| Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor. | |
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MedLine Citation:
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PMID: 23140271 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Grégory Da Costa; Arnaud Bondon; Jérome Coutant; Patrick Curmi; Jean-Pierre Monti |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-11-12 |
Journal Detail:
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Title: Journal of biomolecular structure & dynamics Volume: - ISSN: 1538-0254 ISO Abbreviation: J. Biomol. Struct. Dyn. Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-11-12 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8404176 Medline TA: J Biomol Struct Dyn Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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a Laboratoire de physique et biophysique , Université de Bordeaux Victor Segalen, GESVAB EA 3675, ISVV , 146 rue Léo Saignat , Bordeaux cedex , 33076 , France. |
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