1plw
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1plx|1PLX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1plw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plw OCA], [http://www.ebi.ac.uk/pdbsum/1plw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1plw RCSB]</span> | ||
}} | }} | ||
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[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:26 2008'' |
Revision as of 20:01, 30 March 2008
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| Related: | 1PLX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structure of Methionine-Enkephalin in fast tumbling DMPC/DHPC bicelles
Overview
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
1PLW is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
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