1MYU
Lipid induced conformation of the tachykinin peptide Kassinin
Summary for 1MYU
| Entry DOI | 10.2210/pdb1myu/pdb |
| NMR Information | BMRB: 5574 |
| Descriptor | Kassinin (1 entity in total) |
| Functional Keywords | helical core, 3-10 helix, lipid induced conformation, dpc micelles, neuropeptide |
| Biological source | Kassina senegalensis |
| Total number of polymer chains | 1 |
| Total formula weight | 1336.53 |
| Authors | Grace, R.C.,Lynn, A.M.,Cowsik, S.M. (deposition date: 2002-10-04, release date: 2002-10-16, Last modification date: 2024-05-01) |
| Primary citation | Grace, R.C.,Lynn, A.M.,Cowsik, S.M. Lipid induced conformation of the tachykinin peptide Kassinin. J.Biomol.Struct.Dyn., 18:611-21, 623-5-611-21, 623-5, 2001 Cited by PubMed Abstract: Both the aqueous and lipid-induced structure of Kassinin, a dodecapeptide of amphibian origin, has been studied by two-dimensional proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy and distance geometry calculations. 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 in a distance geometry algorithm to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that, while in water Kassinin prefers to be in an extended chain conformation, in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system, helical conformation is induced in the central core and C-terminal region (K4-M12) of the peptide. N-terminus though less defined also displays some degree of order and a possible turn structure. The conformation adopted by Kassinin in the presence of DPC micelles is consistent with the structural motif typical of neurokinin-1 selective agonists and with that reported for Eledoisin in hydrophobic environment. PubMed: 11245256DOI: 10.1080/07391102.2001.10506693 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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