2oyw: Difference between revisions

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[[Image:2oyw.jpg|left|200px]]<br /><applet load="2oyw" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2oyw.jpg|left|200px]]
caption="2oyw" />
 
'''Neurotensin in TFE:H2O (80:20)'''<br />
{{Structure
|PDB= 2oyw |SIZE=350|CAPTION= <scene name='initialview01'>2oyw</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''Neurotensin in TFE:H2O (80:20)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2OYW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OYW OCA].  
2OYW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OYW OCA].  


==Reference==
==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:[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://www.ncbi.nlm.nih.gov/pubmed/17441729 17441729]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Coutant, J.]]
[[Category: Coutant, J.]]
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[[Category: extended structure]]
[[Category: extended structure]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:15 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:06:23 2008''

Revision as of 16:06, 20 March 2008

File:2oyw.jpg


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2oyw
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Neurotensin in TFE:H2O (80:20)


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

2OYW 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

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