1nrj: Difference between revisions

Revision as of 08:21, 29 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:1nrj.png

Template:STRUCTURE 1nrj

Signal Recognition Particle Receptor Beta-Subunit in Complex with the SRX Domain from the Alpha-SubunitSignal Recognition Particle Receptor Beta-Subunit in Complex with the SRX Domain from the Alpha-Subunit

Template:ABSTRACT PUBMED 12654246

About this StructureAbout this Structure

1NRJ is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor., Schwartz T, Blobel G, Cell. 2003 Mar 21;112(6):793-803. PMID:12654246

Page seeded by OCA on Tue Jul 29 08:21:11 2008

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OCA

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-[[Image:1nrj.gif|left|200px]]
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 {{STRUCTURE_1nrj|  PDB=1nrj  |  SCENE=  }}
-'''Signal Recognition Particle Receptor Beta-Subunit in Complex with the SRX Domain from the Alpha-Subunit'''
+===Signal Recognition Particle Receptor Beta-Subunit in Complex with the SRX Domain from the Alpha-Subunit===
-==Overview==
+<!--
-Protein translocation across and insertion into membranes is a process essential to all life forms. In higher eukaryotes, this process is initiated by targeting the translating ribosome to the endoplasmic reticulum via the signal recognition particle (SRP) and its membrane-associated heterodimeric receptor (SR). This targeting step is regulated by three G proteins, SRP54, SR alpha, and SR beta, which act in concert. Little is known about the regulatory role of SR beta. Here, we present the 1.7 A crystal structure of the SR beta-GTP subunit in complex with the interaction domain of SR alpha. Strikingly, the binding interface overlaps largely with the switch 1 region of SR beta. This finding, together with additional biochemical data, shows that the eukaryotic SR is a conditional and not an obligate heterodimer. The results suggest that the GTP/GDP switch cycle of SR beta functions as a regulatory switch for the receptor dimerization. We discuss the implications for the translocation pathway.
+The line below this paragraph, {{ABSTRACT_PUBMED_12654246}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12654246 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12654246}}
 ==About this Structure==
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 [[Category: Signal recognition particle]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:53:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:21:11 2008''