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1PLW

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

Summary for 1PLW
Entry DOI10.2210/pdb1plw/pdb
Related1PLX
NMR InformationBMRB: 5915
DescriptorMet-enkephalin 1 (1 entity in total)
Functional Keywordsneuropeptide
Cellular locationSecreted: P01210
Total number of polymer chains1
Total formula weight573.66
Authors
Marcotte, I.,Separovic, F.,Auger, M.,Gagne, S.M. (deposition date: 2003-06-09, release date: 2004-03-16, Last modification date: 2024-05-22)
Primary citationMarcotte, I.,Separovic, F.,Auger, M.,Gagne, S.M.
A multidimensional (1)h NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles.
Biophys.J., 86:1587-1600, 2004
Cited by
PubMed Abstract: 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.
PubMed: 14990485
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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