1n6t: Difference between revisions

Revision as of 15:02, 21 February 2008

Solution Structure of the Tachykinin Peptide Neurokinin A

OverviewOverview

The solution structure of NKA, a decapeptide of mammalian origin, has been characterized by CD spectropolarimetry and 2D proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy in both aqueous and membrane mimetic solvents. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The distance constraints obtained from the NMR data have been utilized to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that in water NKA prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region (D4-M10) of the peptide in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system. Though less defined the N-terminus also displays some degree of order and a possible turn structure. The conformation adopted by NKA in the presence of DPC micelles represents a structural motif typical of neurokinin-2 selective agonists and is similar to that reported for eledoisin in hydrophobic environment.

About this StructureAbout this Structure

1N6T is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles., Chandrashekar IR, Cowsik SM, Biophys J. 2003 Dec;85(6):4002-11. PMID:14645089

Page seeded by OCA on Thu Feb 21 14:02:53 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1n6t.jpg|left|200px]]<br /><applet load="1n6t" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1n6t.jpg|left|200px]]<br /><applet load="1n6t" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1n6t" />
 '''Solution Structure of the Tachykinin Peptide Neurokinin A'''<br />
 ==Overview==
-The solution structure of NKA, a decapeptide of mammalian origin, has been, characterized by CD spectropolarimetry and 2D proton nuclear magnetic, resonance (2D 1H-NMR) spectroscopy in both aqueous and membrane mimetic, solvents. Unambiguous NMR assignments of protons have been made with the, aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and, nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The, distance constraints obtained from the NMR data have been utilized to, generate a family of structures, which have been refined using restrained, energy minimization and dynamics. These data show that in water NKA, prefers to be in an extended chain conformation whereas a helical, conformation is induced in the central core and the C-terminal region, (D4-M10) of the peptide in the presence of perdeuterated, dodecylphosphocholine (DPC) micelles, a membrane model system. Though less, defined the N-terminus also displays some degree of order and a possible, turn structure. The conformation adopted by NKA in the presence of DPC, micelles represents a structural motif typical of neurokinin-2 selective, agonists and is similar to that reported for eledoisin in hydrophobic, environment.
+The solution structure of NKA, a decapeptide of mammalian origin, has been characterized by CD spectropolarimetry and 2D proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy in both aqueous and membrane mimetic solvents. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The distance constraints obtained from the NMR data have been utilized to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that in water NKA prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region (D4-M10) of the peptide in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system. Though less defined the N-terminus also displays some degree of order and a possible turn structure. The conformation adopted by NKA in the presence of DPC micelles represents a structural motif typical of neurokinin-2 selective agonists and is similar to that reported for eledoisin in hydrophobic environment.
 ==About this Structure==
-N6T 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N6T OCA].
+N6T 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=1N6T OCA].
 ==Reference==
 Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles., Chandrashekar IR, Cowsik SM, Biophys J. 2003 Dec;85(6):4002-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14645089 14645089]
 [[Category: Single protein]]
-[[Category: Chandrashekar, I.R.]]
+[[Category: Chandrashekar, I R.]]
-[[Category: Cowsik, S.M.]]
+[[Category: Cowsik, S M.]]
 [[Category: 3 10 helix]]
 [[Category: dpc micelles]]
@@ Line 19: / Line 19: @@
 [[Category: lipid induced conformation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:00:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:53 2008''