2go5: Difference between revisions

Revision as of 12:30, 27 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:2go5.png

Template:STRUCTURE 2go5

Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complexStructure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex

Template:ABSTRACT PUBMED 16675701

About this StructureAbout this Structure

2GO5 is a Protein complex structure of sequences from Canis sp., Homo sapiens, Mus musculus and Triticum sp.. Full crystallographic information is available from OCA.

ReferenceReference

Signal recognition particle receptor exposes the ribosomal translocon binding site., Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R, Science. 2006 May 5;312(5774):745-7. PMID:16675701

Page seeded by OCA on Sun Jul 27 12:30:24 2008

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

OCA

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-'''Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex'''
+===Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex===
-==Overview==
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-Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted.
+The line below this paragraph, {{ABSTRACT_PUBMED_16675701}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16675701}}
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 [[Category: Sr]]
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