2nou
From Proteopedia
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| - | [[Image:2nou.gif|left|200px]] | + | [[Image:2nou.gif|left|200px]] |
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| - | '''Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist''' | + | {{Structure |
| + | |PDB= 2nou |SIZE=350|CAPTION= <scene name='initialview01'>2nou</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NOU is a [ | + | 2NOU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15731392 15731392] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cowsik, S M.]] | [[Category: Cowsik, S M.]] | ||
[[Category: Dike, A.]] | [[Category: Dike, A.]] | ||
[[Category: 3-10 helix]] | [[Category: 3-10 helix]] | ||
| - | [[Category: dpc | + | [[Category: dpc micelle]] |
[[Category: helix]] | [[Category: helix]] | ||
[[Category: lipid induced conformation]] | [[Category: lipid induced conformation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:49:08 2008'' |
Revision as of 15:49, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 17:49:08 2008
