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| - | [[Image:2gfr.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2gfr.png|left|200px]] |
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| | {{STRUCTURE_2gfr| PDB=2gfr | SCENE= }} | | {{STRUCTURE_2gfr| PDB=2gfr | SCENE= }} |
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| - | '''Solution structure of Amphibian tachykinin Uperolein bound to DPC micelles'''
| + | ===Solution structure of Amphibian tachykinin Uperolein bound to DPC micelles=== |
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| - | ==Overview==
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| - | Uperolein, a physalaemin-like endecapeptide, has been shown to be selective for Neurokinin 1 receptor. As a first step towards understanding the structure-activity relationship, we report the membrane-induced structure of Uperolein with the aid of circular dichroism and 2D (1)H NMR spectroscopy. Sequence-specific resonance assignments of protons have been made using 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 torsion angle molecular dynamics within program DYANA. The conformational range of the peptide revealed by NMR and CD studies has been analysed in terms of characteristic secondary features. Analysis of NMR data indicates that the global fold of Uperolein can be explained in terms of equilibrium between 3(10)-helix and alpha-helix from residues 5 to 11. An extended highly flexible N-terminus displays some degree of order and a possible turn structure. A comparison between the structures of Uperolein and Substance P, a prototype and endogenous Neurokinin 1 receptor agonist, indicates several common features in the distribution of hydrophobic and hydrophilic residues. Both the peptides show an amphiphilic character towards the middle region. The similarities suggest that the molecules interact with the receptor in an analogous manner.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16979908}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16979908 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16979908}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2GFR is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GFR OCA]. | + | 2GFR is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GFR 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 05:03:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:27:02 2008'' |
Revision as of 18:27, 28 July 2008
Template:STRUCTURE 2gfr
Solution structure of Amphibian tachykinin Uperolein bound to DPC micelles
Template:ABSTRACT PUBMED 16979908
About this Structure
2GFR is a Single protein structure. Full experimental information is available from OCA.
Reference
Solution structure of amphibian tachykinin Uperolein bound to DPC micelles., Dike A, Cowsik SM, J Struct Biol. 2006 Dec;156(3):442-52. Epub 2006 Aug 1. PMID:16979908
Page seeded by OCA on Mon Jul 28 21:27:02 2008
