1edw: Difference between revisions

Revision as of 00:32, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1edw.png

Template:STRUCTURE 1edw

SOLUTION STRUCTURE OF THIRD INTRADISKAL LOOP OF BOVINE RHODOPSIN (RESIDUES 268-293)SOLUTION STRUCTURE OF THIRD INTRADISKAL LOOP OF BOVINE RHODOPSIN (RESIDUES 268-293)

Template:ABSTRACT PUBMED 10888202

About this StructureAbout this Structure

1EDW is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 00:32:52 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1edw.gif|left|200px]]
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 {{STRUCTURE_1edw|  PDB=1edw  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THIRD INTRADISKAL LOOP OF BOVINE RHODOPSIN (RESIDUES 268-293)'''
+===SOLUTION STRUCTURE OF THIRD INTRADISKAL LOOP OF BOVINE RHODOPSIN (RESIDUES 268-293)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10888202}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10888202 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10888202}}
 ==About this Structure==
-EDW is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDW OCA].
+EDW is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDW OCA].
 ==Reference==
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 [[Category: Yeagle, P L.]]
 [[Category: Helix-turn-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:58:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:32:52 2008''