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2oyw

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(New page: 200px<br /><applet load="2oyw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oyw" /> '''Neurotensin in TFE:H2O (80:20)'''<br /> ==O...)
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[[Image:2oyw.jpg|left|200px]]<br /><applet load="2oyw" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2oyw" />
 
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'''Neurotensin in TFE:H2O (80:20)'''<br />
 
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==Overview==
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==Neurotensin in TFE:H2O (80:20)==
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Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple, biological functions in the central and peripheral nervous system. Little, is known about the structure of this neuropeptide, and what is known only, concerns its C-terminal part. We determined here for the first time the, structure of the full-length NT in membrane-mimicking environments by, means of classical proton-proton distance constraints derived from, solution-state NMR spectroscopy. NT was found to have a structure at both, its N and C termini, whereas the central region of NT remains highly, flexible. In TFE and HFIP solutions, the NT C-terminus presents an, extended slightly incurved structure, whereas in DPC it has a beta turn., The N-terminal region of NT possesses great adaptability and accessibility, to the microenvironment in the three media studied. Altogether, our work, demonstrates a structure of NT fully compatible with its NTR-bound state.
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<StructureSection load='2oyw' size='340' side='right'caption='[[2oyw]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2oyw]] is a 1 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=2OYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OYW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyw OCA], [https://pdbe.org/2oyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oyw RCSB], [https://www.ebi.ac.uk/pdbsum/2oyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oyw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NEUT_HUMAN NEUT_HUMAN] Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple biological functions in the central and peripheral nervous system. Little is known about the structure of this neuropeptide, and what is known only concerns its C-terminal part. We determined here for the first time the structure of the full-length NT in membrane-mimicking environments by means of classical proton-proton distance constraints derived from solution-state NMR spectroscopy. NT was found to have a structure at both its N and C termini, whereas the central region of NT remains highly flexible. In TFE and HFIP solutions, the NT C-terminus presents an extended slightly incurved structure, whereas in DPC it has a beta turn. The N-terminal region of NT possesses great adaptability and accessibility to the microenvironment in the three media studied. Altogether, our work demonstrates a structure of NT fully compatible with its NTR-bound state.
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==About this Structure==
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NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition.,Coutant J, Curmi PA, Toma F, Monti JP Biochemistry. 2007 May 15;46(19):5656-63. Epub 2007 Apr 19. PMID:17441729<ref>PMID:17441729</ref>
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2OYW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OYW OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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NMR Solution Structure of Neurotensin in Membrane-Mimetic Environments: Molecular Basis for Neurotensin Receptor Recognition., Coutant J, Curmi PA, Toma F, Monti JP, Biochemistry. 2007 May 15;46(19):5656-5663. Epub 2007 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17441729 17441729]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2oyw" style="background-color:#fffaf0;"></div>
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[[Category: Coutant, J.]]
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== References ==
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[[Category: Curmi, P.A.]]
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<references/>
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[[Category: Monti, J.P.]]
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__TOC__
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[[Category: extended structure]]
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</StructureSection>
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[[Category: Homo sapiens]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:47 2008''
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[[Category: Large Structures]]
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[[Category: Coutant J]]
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[[Category: Curmi PA]]
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[[Category: Monti JP]]

Current revision

Neurotensin in TFE:H2O (80:20)

PDB ID 2oyw

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