2oyw: Difference between revisions
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New page: left|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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== | ==Neurotensin in TFE:H2O (80:20)== | ||
Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple | <StructureSection load='2oyw' size='340' side='right'caption='[[2oyw]]' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 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=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> | |||
</table> | |||
== Function == | |||
[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: | <div class="pdbe-citations 2oyw" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Coutant J]] | |||
[[Category: Curmi PA]] | |||
[[Category: Monti JP]] | |||
Latest revision as of 01:17, 21 November 2024
Neurotensin in TFE:H2O (80:20)
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