Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles |
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Authors: | Chandrashekar Indu R Cowsik Sudha M |
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Affiliation: | School of Life Sciences, Jawaharlal Nehru University, New Delhi 110 067, India. |
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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. |
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Keywords: | NKA, neurokinin A DPC, dodecylphosphocholine CD, circular dichroism DQF-COSY, double-quantum filtered correlation spectroscopy NOESY, 2D nuclear Overhauser effect spectroscopy ROESY, rotating frame Overhauser effect spectroscopy TOCSY, total correlation spectroscopy NK, neurokinin NKB, neurokinin B NPK, neuropeptide K NPγ, neuropeptide gamma |
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