1PLX

NMR structure of Methionine-Enkephalin in fast tumbling Bicelles/DMPG

1PLX の概要

• エントリーDOI: 10.2210/pdb1plx/pdb
• 関連するPDBエントリー: 1PLW
• NMR情報: BMRB: 5914
• 分子名称: Met-enkephalin 1 (1 entity in total)
• 機能のキーワード: neuropeptide
• 細胞内の位置: Secreted: P01210
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 573.66

構造登録者

Marcotte, I.,Separovic, F.,Auger, M.,Gagne, S.M. (登録日: 2003-06-09, 公開日: 2004-03-16, 最終更新日: 2024-05-22)

主引用文献

Marcotte, 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

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

実験手法

SOLUTION NMR