1mxq
From Proteopedia
(New page: 200px<br /><applet load="1mxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mxq" /> '''Solution Structure of the Tachykinin Peptide...) |
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'''Solution Structure of the Tachykinin Peptide Eledoisin'''<br /> | '''Solution Structure of the Tachykinin Peptide Eledoisin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Both the aqueous and the lipid-induced structure of eledoisin, an | + | Both the aqueous and the lipid-induced structure of eledoisin, an undecapeptide of mollusk origin, have been studied by two-dimensional proton nuclear magnetic resonance spectroscopy and distance geometry calculations. Unambiguous nuclear magnetic resonance assignments of protons have been made with the aid of correlation spectroscopy experiments and nuclear Overhauser effect spectroscopy experiments. The distance constraints obtained from the nuclear magnetic resonance data have been utilized in a distance geometry algorithm to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that, while in water and dimethyl sulfoxide, eledoisin prefers to be in an extended chain conformation, whereas in the presence of perdeuterated dodecylphosphocholine micelles, a membrane model system, helical conformation is induced in the central core and C-terminal region (K4-M11) of the peptide. N terminus, though less defined, also displays some degree of order and a possible turn structure. The conformation adopted by eledoisin in the presence of dodecylphosphocholine micelles is similar to the structural motif typical of neurokinin-2 selective agonists and with that reported for kassinin in hydrophobic environment. |
==About this Structure== | ==About this Structure== | ||
| - | 1MXQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1MXQ is a [http://en.wikipedia.org/wiki/Single_protein 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=1MXQ OCA]. |
==Reference== | ==Reference== | ||
Solution structure of the tachykinin peptide eledoisin., Grace RC, Chandrashekar IR, Cowsik SM, Biophys J. 2003 Jan;84(1):655-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12524318 12524318] | Solution structure of the tachykinin peptide eledoisin., Grace RC, Chandrashekar IR, Cowsik SM, Biophys J. 2003 Jan;84(1):655-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12524318 12524318] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chandrashekar, I | + | [[Category: Chandrashekar, I R.]] |
| - | [[Category: Cowsik, S | + | [[Category: Cowsik, S M.]] |
| - | [[Category: Grace, R | + | [[Category: Grace, R C.]] |
[[Category: 3 10 helix]] | [[Category: 3 10 helix]] | ||
[[Category: dpc micelles]] | [[Category: dpc micelles]] | ||
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[[Category: lipid induced conformation]] | [[Category: lipid induced conformation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:09 2008'' |
Revision as of 12:00, 21 February 2008
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Solution Structure of the Tachykinin Peptide Eledoisin
Overview
Both the aqueous and the lipid-induced structure of eledoisin, an undecapeptide of mollusk origin, have been studied by two-dimensional proton nuclear magnetic resonance spectroscopy and distance geometry calculations. Unambiguous nuclear magnetic resonance assignments of protons have been made with the aid of correlation spectroscopy experiments and nuclear Overhauser effect spectroscopy experiments. The distance constraints obtained from the nuclear magnetic resonance data have been utilized in a distance geometry algorithm to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that, while in water and dimethyl sulfoxide, eledoisin prefers to be in an extended chain conformation, whereas in the presence of perdeuterated dodecylphosphocholine micelles, a membrane model system, helical conformation is induced in the central core and C-terminal region (K4-M11) of the peptide. N terminus, though less defined, also displays some degree of order and a possible turn structure. The conformation adopted by eledoisin in the presence of dodecylphosphocholine micelles is similar to the structural motif typical of neurokinin-2 selective agonists and with that reported for kassinin in hydrophobic environment.
About this Structure
1MXQ is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of the tachykinin peptide eledoisin., Grace RC, Chandrashekar IR, Cowsik SM, Biophys J. 2003 Jan;84(1):655-64. PMID:12524318
Page seeded by OCA on Thu Feb 21 14:00:09 2008
