1n6t

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1n6t

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Solution Structure of the Tachykinin Peptide Neurokinin A

Overview

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.

About this Structure

1N6T is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles., Chandrashekar IR, Cowsik SM, Biophys J. 2003 Dec;85(6):4002-11. PMID:14645089

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