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Crystal structure of the Smaug RNA binding domainCrystal structure of the Smaug RNA binding domain
Structural highlights
Function[SMG_DROME] Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevent their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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