2gfr
From Proteopedia
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| - | [[Image:2gfr.gif|left|200px]] | + | [[Image:2gfr.gif|left|200px]] |
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| - | '''Solution structure of Amphibian tachykinin Uperolein bound to DPC micelles''' | + | {{Structure |
| + | |PDB= 2gfr |SIZE=350|CAPTION= <scene name='initialview01'>2gfr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of Amphibian tachykinin Uperolein bound to DPC micelles''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GFR is a [ | + | 2GFR 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=2GFR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16979908 16979908] |
[[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 17:04:08 2008'' |
Revision as of 15:04, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of Amphibian tachykinin Uperolein bound to DPC micelles
Overview
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.
About this Structure
2GFR is a Single protein structure of sequence from [1]. Full crystallographic 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 Thu Mar 20 17:04:08 2008
