1ekz

NMR STRUCTURE OF THE COMPLEX BETWEEN THE THIRD DSRBD FROM DROSOPHILA STAUFEN AND A RNA HAIRPINNMR STRUCTURE OF THE COMPLEX BETWEEN THE THIRD DSRBD FROM DROSOPHILA STAUFEN AND A RNA HAIRPIN

Structural highlights 1ekz is a 2 chain structure with sequence from Drosophila melanogaster. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function STAU_DROME Required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. Osk protein is required to keep osk RNA and stau protein at the posterior pole. Stau-bcd complexes form particles that show a microtubule-dependent localization. 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 PubMed The double-stranded RNA-binding domain (dsRBD) is a common RNA-binding motif found in many proteins involved in RNA maturation and localization. To determine how this domain recognizes RNA, we have studied the third dsRBD from Drosophila Staufen. The domain binds optimally to RNA stem-loops containing 12 uninterrupted base pairs, and we have identified the amino acids required for this interaction. By mutating these residues in a staufen transgene, we show that the RNA-binding activity of dsRBD3 is required in vivo for Staufen-dependent localization of bicoid and oskar mRNAs. Using high-resolution NMR, we have determined the structure of the complex between dsRBD3 and an RNA stem-loop. The dsRBD recognizes the shape of A-form dsRNA through interactions between conserved residues within loop 2 and the minor groove, and between loop 4 and the phosphodiester backbone across the adjacent major groove. In addition, helix alpha1 interacts with the single-stranded loop that caps the RNA helix. Interactions between helix alpha1 and single-stranded RNA may be important determinants of the specificity of dsRBD proteins. RNA recognition by a Staufen double-stranded RNA-binding domain.,Ramos A, Grunert S, Adams J, Micklem DR, Proctor MR, Freund S, Bycroft M, St Johnston D, Varani G EMBO J. 2000 Mar 1;19(5):997-1009. PMID:10698941 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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