This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1aqg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1aqg.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1aqg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1aqg| PDB=1aqg | SCENE= }}
{{STRUCTURE_1aqg| PDB=1aqg | SCENE= }}
-
'''NMR STRUCTURE OF THE RHODOPSIN-BOUND C-TERMINAL PEPTIDE OF THE TRANSDUCIN ALPHA-SUBUNIT, 20 STRUCTURES'''
+
===NMR STRUCTURE OF THE RHODOPSIN-BOUND C-TERMINAL PEPTIDE OF THE TRANSDUCIN ALPHA-SUBUNIT, 20 STRUCTURES===
-
==Overview==
+
<!--
-
A large superfamily of transmembrane receptors control cellular responses to diverse extracellular signals by catalyzing activation of specific types of heterotrimeric GTP-binding proteins. How these receptors recognize and promote nucleotide exchange on G protein alpha subunits to initiate signal amplification is unknown. The three-dimensional structure of the transducin (Gt) alpha subunit C-terminal undecapeptide Gtalpha(340-350) IKENLKDCGLF was determined by transferred nuclear Overhauser effect spectroscopy while it was bound to photoexcited rhodopsin. Light activation of rhodopsin causes a dramatic shift from a disordered conformation of Gtalpha(340-350) to a binding motif with a helical turn followed by an open reverse turn centered at Gly-348, a helix-terminating C capping motif of an alphaL type. Docking of the NMR structure to the GDP-bound x-ray structure of Gt reveals that photoexcited rhodopsin promotes the formation of a continuous helix over residues 325-346 terminated by the C-terminal helical cap with a unique cluster of crucial hydrophobic side chains. A molecular mechanism by which activated receptors can control G proteins through reversible conformational changes at the receptor-G protein interface is demonstrated.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9539726}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9539726 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9539726}}
==About this Structure==
==About this Structure==
-
1AQG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQG OCA].
+
1AQG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQG OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Transducer]]
[[Category: Transducer]]
[[Category: Transducin]]
[[Category: Transducin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:35:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:24:44 2008''

Revision as of 14:24, 30 June 2008

Image:1aqg.png

Template:STRUCTURE 1aqg

NMR STRUCTURE OF THE RHODOPSIN-BOUND C-TERMINAL PEPTIDE OF THE TRANSDUCIN ALPHA-SUBUNIT, 20 STRUCTURES

Template:ABSTRACT PUBMED 9539726

About this Structure

1AQG is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

Reference

Light-activated rhodopsin induces structural binding motif in G protein alpha subunit., Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4270-5. PMID:9539726

Page seeded by OCA on Mon Jun 30 17:24:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aqg"
Personal tools