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==Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor==
<StructureSection load='2lyw' size='340' side='right'caption='[[2lyw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lyw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LYW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lyw OCA], [https://pdbe.org/2lyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lyw RCSB], [https://www.ebi.ac.uk/pdbsum/2lyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lyw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NTR1_HUMAN NTR1_HUMAN] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.
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== 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<ref>PMID:23140271</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2lyw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Da Costa G]]
[[Category: Monti J]]