2oyv

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(New page: 200px<br /><applet load="2oyv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oyv" /> '''Neurotensin in DPC micelles'''<br /> ==Over...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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]
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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: Protein complex]]
[[Category: Coutant, J.]]
[[Category: Coutant, J.]]
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[[Category: Curmi, P.A.]]
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[[Category: Curmi, P A.]]
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[[Category: Monti, J.P.]]
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[[Category: Monti, J P.]]
[[Category: type i turn]]
[[Category: type i turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:04 2008''

Revision as of 16:24, 21 February 2008


2oyv

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Neurotensin in DPC micelles

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.

About this Structure

2OYV is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

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):5656-63. Epub 2007 Apr 19. PMID:17441729

Page seeded by OCA on Thu Feb 21 18:24:04 2008

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