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[[Image:1plw.gif|left|200px]]
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{{STRUCTURE_1plw|  PDB=1plw  |  SCENE=  }}
'''NMR structure of Methionine-Enkephalin in fast tumbling DMPC/DHPC bicelles'''


==NMR structure of Methionine-Enkephalin in fast tumbling DMPC/DHPC bicelles==
<StructureSection load='1plw' size='340' side='right'caption='[[1plw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1plw]] 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=1PLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1plw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plw OCA], [https://pdbe.org/1plw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plw RCSB], [https://www.ebi.ac.uk/pdbsum/1plw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PENK_HUMAN PENK_HUMAN] Met- and Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. PENK(114-133) and PENK(237-258) increase glutamate release in the striatum. PENK(114-133) decreases GABA concentration in the striatum.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enkephalins are pentapeptides found in the central nervous system. It is believed that these neuropeptides interact with the nerve cell membrane to adopt a conformation suitable for their binding to an opiate receptor. In this work, we have determined the three-dimensional structure of methionine-enkephalin (Menk) in fast-tumbling bicelles using multidimensional (1)H NMR. Bicelles were selected as model membranes because both their bilayer organization and composition resemble those of natural biomembranes. The effect of the membrane composition on the peptide conformation was explored using both zwitterionic (PC bicelles) and negatively charged bicelles (Bic/PG). Pulsed field gradient experiments allowed the determination of the proportion of Menk bound to the model membranes. Approximately 60% of the water-soluble enkephalin was found to associate to the bicellar systems. Structure calculations from torsion angle and NOE-based distance constraints suggest the presence of both micro - and delta-selective conformers of Menk in each system and slightly different conformers in PC bicelles and Bic/PG. As opposed to previous studies of enkephalins in membrane mimetic systems, our results show that these opiate peptides could adopt several conformations in a membrane environment, which is consistent with the flexibility and poor selectivity of enkephalins.


==Overview==
A multidimensional 1H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles.,Marcotte I, Separovic F, Auger M, Gagne SM Biophys J. 2004 Mar;86(3):1587-600. PMID:14990485<ref>PMID:14990485</ref>
Enkephalins are pentapeptides found in the central nervous system. It is believed that these neuropeptides interact with the nerve cell membrane to adopt a conformation suitable for their binding to an opiate receptor. In this work, we have determined the three-dimensional structure of methionine-enkephalin (Menk) in fast-tumbling bicelles using multidimensional (1)H NMR. Bicelles were selected as model membranes because both their bilayer organization and composition resemble those of natural biomembranes. The effect of the membrane composition on the peptide conformation was explored using both zwitterionic (PC bicelles) and negatively charged bicelles (Bic/PG). Pulsed field gradient experiments allowed the determination of the proportion of Menk bound to the model membranes. Approximately 60% of the water-soluble enkephalin was found to associate to the bicellar systems. Structure calculations from torsion angle and NOE-based distance constraints suggest the presence of both micro - and delta-selective conformers of Menk in each system and slightly different conformers in PC bicelles and Bic/PG. As opposed to previous studies of enkephalins in membrane mimetic systems, our results show that these opiate peptides could adopt several conformations in a membrane environment, which is consistent with the flexibility and poor selectivity of enkephalins.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PLW is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLW OCA].
</div>
<div class="pdbe-citations 1plw" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
A multidimensional 1H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles., Marcotte I, Separovic F, Auger M, Gagne SM, Biophys J. 2004 Mar;86(3):1587-600. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14990485 14990485]
*[[Enkephalin 3D structures|Enkephalin 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Auger, M.]]
<references/>
[[Category: Gagne, S M.]]
__TOC__
[[Category: Marcotte, I.]]
</StructureSection>
[[Category: Separovic, F.]]
[[Category: Homo sapiens]]
[[Category: Peptide]]
[[Category: Large Structures]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:14:07 2008''
[[Category: Auger M]]
[[Category: Gagne SM]]
[[Category: Marcotte I]]
[[Category: Separovic F]]

Latest revision as of 18:56, 29 November 2023

NMR structure of Methionine-Enkephalin in fast tumbling DMPC/DHPC bicelles

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