2NOU

Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist

2NOU の概要

• エントリーDOI: 10.2210/pdb2nou/pdb
• 関連するPDBエントリー: 2NOR
• 分子名称: Scyliorhinin I (1 entity in total)
• 機能のキーワード: helix, 3-10 helix, lipid induced conformation, dpc micelles, neuropeptide
• 細胞内の位置: Secreted: P08608
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1221.47

構造登録者

Dike, A.,Cowsik, S.M. (登録日: 2006-10-26, 公開日: 2006-11-14, 最終更新日: 2023-12-27)

主引用文献

Dike, A.,Cowsik, S.M.
Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist
Biophys.J., 88:3592-3600, 2005

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: 15731392
DOI: 10.1529/biophysj.104.053231

実験手法

SOLUTION NMR