1mfq
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(New page: 200px<br /> <applet load="1mfq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mfq, resolution 3.10Å" /> '''Crystal Structure A...)
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Revision as of 16:04, 12 November 2007
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Crystal Structure Analysis of a Ternary S-Domain Complex of Human Signal Recognition Particle
Overview
The eukaryotic signal recognition particle (SRP) is a cytoplasmic, ribonucleoprotein particle that targets secretory and membrane proteins to, the endoplasmic reticulum. The binding of SRP54 to the S domain of 7SL RNA, is highly dependent on SRP19. Here we present the crystal structure of a, human SRP ternary complex consisting of SRP19, the M domain of SRP54 and, the S domain of 7SL RNA. Upon binding of the M domain of SRP54 to the 7SL, RNA-SRP19 complex, the asymmetric loop of helix 8 in 7SL RNA collapses., The bases of the four nucleotides in the long strand of the asymmetric, loop continuously stack and interact with the M domain, whereas the two, adenines in the short strand flip out and form two A-minor motifs with, helix 6. This stabilizing interaction is only possible when helix 6 has, been positioned parallel to helix 8 by the prior binding of SRP19 to the, tetraloops of helices 6 and 8. Hence, the crystal structure of the ternary, complex suggests why SRP19 is necessary for the stable binding of SRP54 to, the S domain RNA.
About this Structure
1MFQ is a Protein complex structure of sequences from Homo sapiens with MG and CL as ligands. Full crystallographic information is available from OCA.
Reference
Induced structural changes of 7SL RNA during the assembly of human signal recognition particle., Kuglstatter A, Oubridge C, Nagai K, Nat Struct Biol. 2002 Oct;9(10):740-4. PMID:12244299
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