1nzs
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state== |
| + | <StructureSection load='1nzs' size='340' side='right' caption='[[1nzs]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1nzs]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NZS FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nzs RCSB], [http://www.ebi.ac.uk/pdbsum/1nzs PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Visual arrestin binds to the phosphorylated carboxy-terminal region of rhodopsin to block interactions with transducin and terminate signaling in the rod photoreceptor cells. A synthetic seven-phospho-peptide from the C-terminal region of rhodopsin, Rh(330-348), has been shown to bind arrestin and mimic inhibition of signal transduction. In this study, we examine conformational changes in this synthetic peptide upon binding to arrestin by high-resolution proton nuclear magnetic resonance (NMR). We show that the peptide is completely disordered in solution, but becomes structured upon binding to arrestin. A control, unphosphorylated peptide that fails to bind to arrestin remains highly disordered. Specific NMR distance constraints are used to model the arrestin-bound conformation. The models suggest that the phosphorylated carboxy-terminal region of rhodopsin, Rh(330-348), undergoes significant conformational changes and becomes structured upon binding to arrestin. | ||
| - | + | The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.,Kisselev OG, McDowell JH, Hargrave PA FEBS Lett. 2004 Apr 30;564(3):307-11. PMID:15111114<ref>PMID:15111114</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==See Also== | ==See Also== | ||
*[[Rhodopsin|Rhodopsin]] | *[[Rhodopsin|Rhodopsin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Hargrave, P A.]] | [[Category: Hargrave, P A.]] | ||
[[Category: Kisselev, O G.]] | [[Category: Kisselev, O G.]] | ||
Revision as of 13:31, 28 September 2014
NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state
| |||||||||||
