2nou
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2nou.gif|left|200px]] | [[Image:2nou.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2nou", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2nou| PDB=2nou | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist''' | '''Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2NOU is a [[Single protein]] structure | + | 2NOU is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOU OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 24: | ||
[[Category: Dike, A.]] | [[Category: Dike, A.]] | ||
[[Category: 3-10 helix]] | [[Category: 3-10 helix]] | ||
| - | [[Category: | + | [[Category: Dpc micelle]] |
| - | [[Category: | + | [[Category: Helix]] |
| - | [[Category: | + | [[Category: Lipid induced conformation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:43:10 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:43, 4 May 2008
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. 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 Sun May 4 09:43:10 2008
