2oyv
From Proteopedia
(Difference between revisions)
m (Protected "2oyv" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[ | + | ==Neurotensin in DPC micelles== |
| + | <StructureSection load='2oyv' size='340' side='right' caption='[[2oyv]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2oyv]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OYV FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oyw|2oyw]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oyv RCSB], [http://www.ebi.ac.uk/pdbsum/2oyv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:17441729</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Coutant, J.]] | [[Category: Coutant, J.]] | ||
[[Category: Curmi, P A.]] | [[Category: Curmi, P A.]] | ||
Revision as of 11:21, 20 October 2014
Neurotensin in DPC micelles
| |||||||||||
