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2nou
From Proteopedia
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Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist
Overview
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.
About this Structure
2NOU is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 Agonist., Dike A, Cowsik SM, Biophys J. 2005 May;88(5):3592-600. Epub 2005 Feb 24. PMID:15731392
Page seeded by OCA on Wed Nov 21 12:49:17 2007
