1nzs

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(New page: 200px<br /><applet load="1nzs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nzs" /> '''NMR structures of phosphorylated carboxy ter...)
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'''NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state'''<br />
'''NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1NZS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NZS OCA].
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1NZS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZS OCA].
==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15111114 15111114]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15111114 15111114]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hargrave, P.A.]]
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[[Category: Hargrave, P A.]]
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[[Category: Kisselev, O.G.]]
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[[Category: Kisselev, O G.]]
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[[Category: McDowell, J.H.]]
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[[Category: McDowell, J H.]]
[[Category: arrestin]]
[[Category: arrestin]]
[[Category: ball-and-chain]]
[[Category: ball-and-chain]]
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[[Category: signal termination]]
[[Category: signal termination]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:41:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:49 2008''

Revision as of 12:11, 21 February 2008


1nzs

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NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state

Overview

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.

About this Structure

1NZS is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Feb 21 14:11:49 2008

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