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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Crystallization and characterization of Smaug: a novel RNA-binding motif.

During Drosophila embryogenesis, Smaug protein represses translation of Nanos through an interaction with a specific element in its 3(')UTR. The repression occurs in the bulk cytoplasm of the embryo; Nanos is, however, successfully translated in the specialized cytoplasm of the posterior pole. This generates a gradient of Nanos emanating from the posterior pole that is essential for organizing proper abdominal segmentation. To understand the structural basis of RNA binding and translational control, we have crystallized a domain of Drosophila Smaug that binds RNA. The crystals belong to the space group R3 with unit cell dimensions of a=b=129.3A, c=33.1A, alpha=beta=90 degrees, gamma=120 degrees and diffract to 1.80A with synchrotron radiation. Initial characterization of this domain suggests that it encodes a novel RNA-binding motif.[1]


  1. Crystallization and characterization of Smaug: a novel RNA-binding motif. Green, J.B., Edwards, T.A., Trincao, J., Escalante, C.R., Wharton, R.P., Aggarwal, A.K. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
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