1e8s
ALU DOMAIN OF THE MAMMALIAN SRP (POTENTIAL ALU RETROPOSITION INTERMEDIATE)
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OverviewOverview
The Alu domain of the mammalian signal recognition particle (SRP), comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and, 3' terminal sequences of SRP RNA. It retards the ribosomal elongation of, signal-peptide-containing proteins before their engagement with the, translocation machinery in the endoplasmic reticulum. Here we report two, crystal structures of the heterodimer SRP9/14 bound either to the 5', domain or to a construct containing both 5' and 3' domains. We present a, model of the complete Alu domain that is consistent with extensive, biochemical data. SRP9/14 binds strongly to the conserved core of the 5', domain, which forms a U-turn connecting two helical stacks. Reversible, docking of the more weakly bound 3' domain might be functionally important, in the mechanism of translational regulation. The Alu domain structure is, probably conserved in other cytoplasmic ribonucleoprotein particles and, retroposition intermediates containing SRP9/14-bound RNAs transcribed from, Alu repeats or related elements in genomic DNA.
About this StructureAbout this Structure
1E8S is a Protein complex structure of sequences from Homo sapiens with EU3 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure and assembly of the Alu domain of the mammalian signal recognition particle., Weichenrieder O, Wild K, Strub K, Cusack S, Nature. 2000 Nov 9;408(6809):167-73. PMID:11089964
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