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| - | [[Image:2b19.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2b19| PDB=2b19 | SCENE= }} | | {{STRUCTURE_2b19| PDB=2b19 | SCENE= }} |
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| - | '''Solution Structure of mammalian tachykinin peptide, Neuropeptide K'''
| + | ===Solution Structure of mammalian tachykinin peptide, Neuropeptide K=== |
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| - | ==Overview==
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| - | Neuropeptide K (NPK), an N-terminally extended form of neurokinin A (NKA), represents the most potent and longest lasting vasodepressor and cardiomodulatory tachykinin reported thus far. NPK has been shown to have high selectivity for the NK2 receptor. Because the micelle-associated structure may be relevant to the NPK-receptor interaction, the three-dimensional structure of the NPK in aqueous and micellar environments has been studied by two-dimensional proton nuclear magnetic resonance (2D (1)H NMR spectroscopy) and distance geometry calculations. Proton NMR assignments have been carried out with the aid of correlation spectroscopy (DQF-COSY and TOCSY) and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The interproton distances and dihedral angle constraints obtained from the NMR data have been used in torsion angle dynamics algorithm for NMR applications (DYANA) to generate a family of structures, which have been refined using restrained energy minimization and dynamics. The results show that in an aqueous environment NPK lacks a definite secondary structure, although some turn-like elements are present in the N terminus. The structure is well-defined in the presence of dodecylphosphocholine micelles. The global fold of NPK bound to DPC micelles consists of two well-defined helices from residues 9 to 18 and residues 27 to 33 connected by a noncanonical beta turn. The N terminus of the peptide is characterized by a 3(10) helix or a series of dynamic beta turns. The conformational range of the peptide revealed by NMR and circular dichroism (CD) studies has been analyzed in terms of characteristic secondary features. The observed conformational features have been further compared to a NKA and neuropeptide gamma (NPgamma) potent endogenous agonist for the NK2 receptor.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16503654}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16503654 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16503654}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2B19 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B19 OCA]. | + | 2B19 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B19 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 Sat May 3 19:43:44 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:20:46 2008'' |
Revision as of 02:20, 28 July 2008
Template:STRUCTURE 2b19
Solution Structure of mammalian tachykinin peptide, Neuropeptide K
Template:ABSTRACT PUBMED 16503654
About this Structure
2B19 is a Single protein structure. Full experimental information is available from OCA.
Reference
Three-dimensional structure of neuropeptide k bound to dodecylphosphocholine micelles., Dike A, Cowsik SM, Biochemistry. 2006 Mar 7;45(9):2994-3004. PMID:16503654
Page seeded by OCA on Mon Jul 28 05:20:46 2008
