2xsf

Crystal structure of the RRM domain of mouse Deleted in azoospermia- like

spinqualitylabelsall models 2xsf, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xsf is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DAZL_MOUSE RNA-binding protein, which is essential for gametogenesis in both males and females. Plays a central role during spermatogenesis. Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU triplets, and thereby regulating the translation of key transcripts. Publication Abstract from PubMed A defect in germ-cell (sperm and oocyte) development is the leading cause of male and female infertility. Control of translation through the binding of deleted in azoospermia (DAZ)-like (DAZL) to the 3'-UTRs of mRNAs, via a highly conserved RNA recognition motif (RRM), has been shown to be essential in germ-cell development. Crystal structures of the RRM from murine DAZL (Dazl), both alone and in complex with RNA sequences from the 3'-UTRs of mRNAs regulated by Dazl, reveal high-affinity sequence-specific recognition of a GUU triplet involving an extended, kinked, pair of beta-strands. Recognition of the GUU triplet is maintained, whereas the identity and position of bases flanking this triplet varies. The Dazl RRM is thus able to recognize GUU triplets in different sequence contexts. Mutation of bases within the GUU triplet reduces the affinity of binding. Together with the demonstration that multiple Dazl RRMs can bind to a single RNA containing multiple GUU triplets, these structures suggest that the number of DAZL molecules bound to GUU triplets in the 3'-UTR provides a method for modulating the translation of a target RNA. The conservation of RNA binding and structurally important residues between members of the DAZ family, together with the demonstration that mutation of these residues severely impairs RNA binding, indicate that the mode of RNA binding revealed by these structures is conserved in proteins essential for gamete development from flies to humans. Kinked {beta}-strands mediate high-affinity recognition of mRNA targets by the germ-cell regulator DAZL.,Jenkins HT, Malkova B, Edwards TA Proc Natl Acad Sci U S A. 2011 Oct 20. PMID:22021443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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