2XS5

Crystal structure of the RRM domain of mouse Deleted in azoospermia- like in complex with Mvh RNA, UGUUC

2XS5 の概要

• エントリーDOI: 10.2210/pdb2xs5/pdb
• 関連するPDBエントリー: 2XS2 2XS7 2XSF
• 分子名称: DELETED IN AZOOSPERMIA-LIKE, 5'-R(*UP*GP*UP*UP*CP)-3', DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: rna binding protein-rna complex, translation regulation, rna binding protein/rna
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Cytoplasm: Q64368
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 22748.57

構造登録者

Jenkins, H.T.,Edwards, T.A. (登録日: 2010-09-24, 公開日: 2011-10-05, 最終更新日: 2023-12-20)

主引用文献

Jenkins, H.T.,Edwards, T.A.
Kinked Beta-Strands Mediate High-Affinity Recognition of Mrna Targets by the Germ-Cell Regulator Dazl
Proc.Natl.Acad.Sci.USA, 108:18266-, 2011

PubMed Abstract: 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 β-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.

PubMed: 22021443
DOI: 10.1073/PNAS.1105211108

実験手法

X-RAY DIFFRACTION (1.6 Å)