1oxj
Crystal structure of the Smaug RNA binding domain
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OverviewOverview
The Nanos protein gradient in Drosophila, required for proper abdominal, segmentation, is generated in part via translational repression of its, mRNA by Smaug. We report here the crystal structure of the Smaug RNA, binding domain, which shows no sequence homology to any previously, characterized RNA binding motif. The structure reveals an unusual makeup, in which a SAM domain, a common protein-protein interaction module, is, affixed to a pseudo-HEAT repeat analogous topology (PHAT) domain., Unexpectedly, we find through a combination of structural and genetic, analysis that it is primarily the SAM domain that interacts specifically, with the appropriate nanos mRNA regulatory sequence. Therefore, in, addition to their previously characterized roles in protein-protein, interactions, some SAM domains play crucial roles in RNA binding.
About this StructureAbout this Structure
1OXJ is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
RNA recognition via the SAM domain of Smaug., Green JB, Gardner CD, Wharton RP, Aggarwal AK, Mol Cell. 2003 Jun;11(6):1537-48. PMID:12820967
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