[NMR paper] NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
The ribosomal S1 protein (rS1) is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which could be related to fast recognition. Although many ribosome structures were solved in recent years, a high-resolution structure of a two-domain mRNA-binding competent rS1 construct is not yet...
[NMR paper] The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of co
The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Related Articles The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Nat Struct Biol. 2000 Apr;7(4):329-35
Authors: Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G
The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to...
Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2 - Nature.com
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