2oyw: Difference between revisions

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==Overview==

Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple, biological functions in the central and peripheral nervous system. Little, is known about the structure of this neuropeptide, and what is known only, concerns its C-terminal part. We determined here for the first time the, structure of the full-length NT in membrane-mimicking environments by, means of classical proton-proton distance constraints derived from, solution-state NMR spectroscopy. NT was found to have a structure at both, its N and C termini, whereas the central region of NT remains highly, flexible. In TFE and HFIP solutions, the NT C-terminus presents an, extended slightly incurved structure, whereas in DPC it has a beta turn., The N-terminal region of NT possesses great adaptability and accessibility, to the microenvironment in the three media studied. Altogether, our work, demonstrates a structure of NT fully compatible with its NTR-bound state.

Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple biological functions in the central and peripheral nervous system. Little is known about the structure of this neuropeptide, and what is known only concerns its C-terminal part. We determined here for the first time the structure of the full-length NT in membrane-mimicking environments by means of classical proton-proton distance constraints derived from solution-state NMR spectroscopy. NT was found to have a structure at both its N and C termini, whereas the central region of NT remains highly flexible. In TFE and HFIP solutions, the NT C-terminus presents an extended slightly incurved structure, whereas in DPC it has a beta turn. The N-terminal region of NT possesses great adaptability and accessibility to the microenvironment in the three media studied. Altogether, our work demonstrates a structure of NT fully compatible with its NTR-bound state.

==About this Structure==

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==Reference==

NMR ~~Solution Structure~~ of ~~Neurotensin~~ in ~~Membrane~~-~~Mimetic Environments~~: ~~Molecular Basis~~ for ~~Neurotensin Receptor Recognition~~., Coutant J, Curmi PA, Toma F, Monti JP, Biochemistry. 2007 May 15;46(19):5656-~~5663~~. Epub 2007 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17441729 17441729]

NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition., Coutant J, Curmi PA, Toma F, Monti JP, Biochemistry. 2007 May 15;46(19):5656-63. Epub 2007 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17441729 17441729]

[[Category: Protein complex]]

[[Category: Coutant, J.]]

[[Category: Curmi, P.A.]]

[[Category: Curmi, P A.]]

[[Category: Monti, J.P.]]

[[Category: Monti, J P.]]

[[Category: extended structure]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple, biological functions in the central and peripheral nervous system. Little, is known about the structure of this neuropeptide, and what is known only, concerns its C-terminal part. We determined here for the first time the, structure of the full-length NT in membrane-mimicking environments by, means of classical proton-proton distance constraints derived from, solution-state NMR spectroscopy. NT was found to have a structure at both, its N and C termini, whereas the central region of NT remains highly, flexible. In TFE and HFIP solutions, the NT C-terminus presents an, extended slightly incurved structure, whereas in DPC it has a beta turn., The N-terminal region of NT possesses great adaptability and accessibility, to the microenvironment in the three media studied. Altogether, our work, demonstrates a structure of NT fully compatible with its NTR-bound state.
+Neurotensin (NT) is a 13-residue neuropeptide that exerts multiple biological functions in the central and peripheral nervous system. Little is known about the structure of this neuropeptide, and what is known only concerns its C-terminal part. We determined here for the first time the structure of the full-length NT in membrane-mimicking environments by means of classical proton-proton distance constraints derived from solution-state NMR spectroscopy. NT was found to have a structure at both its N and C termini, whereas the central region of NT remains highly flexible. In TFE and HFIP solutions, the NT C-terminus presents an extended slightly incurved structure, whereas in DPC it has a beta turn. The N-terminal region of NT possesses great adaptability and accessibility to the microenvironment in the three media studied. Altogether, our work demonstrates a structure of NT fully compatible with its NTR-bound state.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-NMR Solution Structure of Neurotensin in Membrane-Mimetic Environments: Molecular Basis for Neurotensin Receptor Recognition., Coutant J, Curmi PA, Toma F, Monti JP, Biochemistry. 2007 May 15;46(19):5656-5663. Epub 2007 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17441729 17441729]
+NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition., Coutant J, Curmi PA, Toma F, Monti JP, Biochemistry. 2007 May 15;46(19):5656-63. Epub 2007 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17441729 17441729]
 [[Category: Protein complex]]
 [[Category: Coutant, J.]]
-[[Category: Curmi, P.A.]]
+[[Category: Curmi, P A.]]
-[[Category: Monti, J.P.]]
+[[Category: Monti, J P.]]
 [[Category: extended structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:15 2008''