期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 11, 期 4, 页码 323-329出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb747
关键词
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The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3 poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). We have determined the solution structures of both domains and show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions. They further delineate a distinct surface patch on each domain containing both basic and aromatic residues that interacts with RNA and accounts for the cooperative binding of short oligonucleotides exhibited by the La NTD.
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