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| - | [[Image:2nou.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2nou| PDB=2nou | SCENE= }} | | {{STRUCTURE_2nou| PDB=2nou | SCENE= }} |
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| - | '''Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist'''
| + | ===Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15731392}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15731392 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15731392}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2NOU is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOU OCA]. | + | 2NOU is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOU OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Helix]] | | [[Category: Helix]] |
| | [[Category: Lipid induced conformation]] | | [[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 Tue Jul 29 11:47:42 2008'' |
Revision as of 08:47, 29 July 2008
Template:STRUCTURE 2nou
Membrane induced structure of Scyliorhinin I: A Dual NK1/NK2 agonist
Template:ABSTRACT PUBMED 15731392
About this Structure
2NOU is a Single protein structure. Full experimental 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 Tue Jul 29 11:47:42 2008
