2NOU
Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist
Summary for 2NOU
| Entry DOI | 10.2210/pdb2nou/pdb |
| Related | 2NOR |
| Descriptor | Scyliorhinin I (1 entity in total) |
| Functional Keywords | helix, 3-10 helix, lipid induced conformation, dpc micelles, neuropeptide |
| Cellular location | Secreted: P08608 |
| Total number of polymer chains | 1 |
| Total formula weight | 1221.47 |
| Authors | Dike, A.,Cowsik, S.M. (deposition date: 2006-10-26, release date: 2006-11-14, Last modification date: 2023-12-27) |
| Primary citation | Dike, A.,Cowsik, S.M. Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist Biophys.J., 88:3592-3600, 2005 Cited by PubMed Abstract: Scyliorhinin I, a linear decapeptide, is the only known tachykinin that shows high affinity for both NK-1 and NK-2 binding sites and low affinity for NK-3 binding sites. As a first step to understand the structure-activity relationship, we report the membrane-induced structure of scyliorhinin I with the aid of circular dichroism and 2D-(1)H NMR spectroscopy. Sequence specific resonance assignments of protons have been made from correlation spectroscopy (TOCSY, DQF-COSY) and NOESY spectroscopy. The interproton distance constraints and dihedral angle constraints have been utilized to generate a family of structures using DYANA. The superimposition of 20 final structures has been reported with backbone pairwise root mean-square deviation of 0.38 +/- 0.19 A. The results show that scyliorhinin I exists in a random coil state in aqueous environments, whereas helical conformation is induced toward the C-terminal region of the peptide (D4-M10) in the presence of dodecyl phosphocholine micelles. Analysis of NMR data is suggestive of the presence of a 3(10)-helix that is in equilibrium with an alpha-helix in this region from residue 4 to 10. An extended highly flexible N-terminus of scyliorhinin I displays some degree of order and a possible turn structure. Observed conformational features have been compared with respect to that of substance P and neurokinin A, which are endogenous agonists of NK-1 and NK-2 receptors, respectively. PubMed: 15731392DOI: 10.1529/biophysj.104.053231 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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