The La protein-RNA complex surfaces.

Richard J Maraia; Mark A Bayfield

doi:10.1016/j.molcel.2006.01.004

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The La protein-RNA complex surfaces.

Richard J Maraia·Mark A Bayfield

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Abstract

A recent issue of Molecular Cell reported that the typical nucleic acid binding surfaces of the RRM and winged-helix motifs, although present in the RNA binding protein La, are not used to engage its best-characterized ligand, 3' UUU-OH. Instead, La uses edgewise and backsides of these motifs for UUU-OH recognition, leaving open their typical surfaces for other potential interactions. These observations provide a framework for appreciating the various activities attributed to this ubiquitous nuclear phosphoprotein, which include its principal function, snRNA 3' end protection, in addition to mRNA-related and RNA chaperone-like activities, as well as DNA and chromatin-associated activity.

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Amino Acid Motifs Autoantigens Binding Sites Humans Macromolecular Substances Models, Molecular Protein Binding Protein Conformation RNA Ribonucleoproteins SS-B Antigen Comment Journal Article Review

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Richard J Maraia, Mark A Bayfield. 2006-01-20. The La protein-RNA complex surfaces.. https://doi.org/10.1016/j.molcel.2006.01.004

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