1N6T

Solution Structure of the Tachykinin Peptide Neurokinin A

Summary for 1N6T

• Entry DOI: 10.2210/pdb1n6t/pdb
• NMR Information: BMRB: 5611
• Descriptor: Neurokinin A (1 entity in total)
• Functional Keywords: helix, 3 10 helix, lipid induced conformation, dpc micelles, neuropeptide
• Total number of polymer chains: 1
• Total formula weight: 1136.32

Authors

Chandrashekar, I.R.,Cowsik, S.M. (deposition date: 2002-11-12, release date: 2003-12-16, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR