View source for 1edw


==SOLUTION STRUCTURE OF THIRD INTRADISKAL LOOP OF BOVINE RHODOPSIN (RESIDUES 268-293)==
<StructureSection load='1edw' size='340' side='right'caption='[[1edw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1edw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1edw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edw OCA], [https://pdbe.org/1edw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edw RCSB], [https://www.ebi.ac.uk/pdbsum/1edw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref> 
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== Publication Abstract from PubMed ==
The intradiskal surface of the transmembrane protein, rhodopsin, consists of the amino terminal domain and three loops connecting six of the seven transmembrane helices. This surface corresponds to the extracellular surface of other G-protein receptors. Peptides that represent each of the extramembraneous domains on this surface (three loops and the amino terminus) were synthesized. These peptides also included residues which, based on a hydrophobic plot, could be expected to be part of the transmembrane helix. The structure of each of these peptides in solution was then determined using two-dimensional 1H nuclear magnetic resonance. All peptide domains showed ordered structures in solution. The structures of each of the peptides from intradiskal loops of rhodopsin exhibited a turn in the central region of the peptide. The ends of the peptides show an unwinding of the transmembrane helices to form this turn. The amino terminal domain peptide exhibited alpha-helical regions with breaks and bends at proline residues. This region forms a compact domain. Together, the structures for the loop and amino terminus domains indicate that the intradiskal surface of rhodopsin is ordered. These data further suggest a structural motif for short loops in transmembrane proteins. The ordered structures of these loops, in the absence of the transmembrane helices, indicate that the primary sequences of these loops are sufficient to code for the turn.

Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin.,Yeagle PL, Salloum A, Chopra A, Bhawsar N, Ali L, Kuzmanovski G, Alderfer JL, Albert AD J Pept Res. 2000 Jun;55(6):455-65. PMID:10888202<ref>PMID:10888202</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1edw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Ali L]]
[[Category: Bhawsar N]]
[[Category: Chopra A]]
[[Category: Salloum A]]
[[Category: Yeagle PL]]