1ry1: Difference between revisions

Revision as of 20:47, 28 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:1ry1.png

Template:STRUCTURE 1ry1

Structure of the signal recognition particle interacting with the elongation-arrested ribosomeStructure of the signal recognition particle interacting with the elongation-arrested ribosome

Template:ABSTRACT PUBMED 14985753

About this StructureAbout this Structure

1RY1 is a Protein complex structure of sequences from Homo sapiens, Mus musculus, Thermus aquaticus and Tursiops truncatus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the signal recognition particle interacting with the elongation-arrested ribosome., Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, Frank J, Beckmann R, Nature. 2004 Feb 26;427(6977):808-14. PMID:14985753

Page seeded by OCA on Mon Jul 28 20:47:38 2008

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OCA

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-'''Structure of the signal recognition particle interacting with the elongation-arrested ribosome'''
+===Structure of the signal recognition particle interacting with the elongation-arrested ribosome===
-==Overview==
+<!--
-Cotranslational translocation of proteins across or into membranes is a vital process in all kingdoms of life. It requires that the translating ribosome be targeted to the membrane by the signal recognition particle (SRP), an evolutionarily conserved ribonucleoprotein particle. SRP recognizes signal sequences of nascent protein chains emerging from the ribosome. Subsequent binding of SRP leads to a pause in peptide elongation and to the ribosome docking to the membrane-bound SRP receptor. Here we present the structure of a targeting complex consisting of mammalian SRP bound to an active 80S ribosome carrying a signal sequence. This structure, solved to 12 A by cryo-electron microscopy, enables us to generate a molecular model of SRP in its functional conformation. The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_14985753}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14985753 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14985753}}
 ==About this Structure==
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 [[Category: Rna binding]]
 [[Category: Signal recognition particle]]
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