Document Detail


Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor.
MedLine Citation:
PMID:  23140271     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Grégory Da Costa; Arnaud Bondon; Jérome Coutant; Patrick Curmi; Jean-Pierre Monti
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-12
Journal Detail:
Title:  Journal of biomolecular structure & dynamics     Volume:  -     ISSN:  1538-0254     ISO Abbreviation:  J. Biomol. Struct. Dyn.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8404176     Medline TA:  J Biomol Struct Dyn     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
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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