Article
NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
The EMBO journal - 17 Jul 1995
Bycroft M, Grünert S, Murzin A G, Proctor M, St Johnston D
Abstract excerpt
The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid motif that is found in a variety of proteins that interact with double-stranded (ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase, PKR. Drosophila staufen protein contains five copies of this motif, and the third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR methods, we have...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Computer Graphics
- Drosophila
- Drosophila Proteins
- Hydroxymethylbilane Synthase
- Insect Hormones
- Magnetic Resonance Spectroscopy
- Models, Molecular