1N6T

Solution Structure of the Tachykinin Peptide Neurokinin A

1N6T の概要

• エントリーDOI: 10.2210/pdb1n6t/pdb
• NMR情報: BMRB: 5611
• 分子名称: Neurokinin A (1 entity in total)
• 機能のキーワード: helix, 3 10 helix, lipid induced conformation, dpc micelles, neuropeptide
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1136.32

構造登録者

Chandrashekar, I.R.,Cowsik, S.M. (登録日: 2002-11-12, 公開日: 2003-12-16, 最終更新日: 2024-05-01)

主引用文献

Chandrashekar, I.R.,Cowsik, S.M.
Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles.
Biophys.J., 85:4002-4011, 2003

PubMed Abstract: The solution structure of NKA, a decapeptide of mammalian origin, has been characterized by CD spectropolarimetry and 2D proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy in both aqueous and membrane mimetic solvents. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The distance constraints obtained from the NMR data have been utilized to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that in water NKA prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region (D4-M10) of the peptide in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system. Though less defined the N-terminus also displays some degree of order and a possible turn structure. The conformation adopted by NKA in the presence of DPC micelles represents a structural motif typical of neurokinin-2 selective agonists and is similar to that reported for eledoisin in hydrophobic environment.

PubMed: 14645089
DOI: 10.1016/S0006-3495(03)74814-0

実験手法

SOLUTION NMR