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Crystal structure of a Pumilio homology domain.

Molecular cell | Apr 4, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11336708

Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein.

Pubmed ID: 11336708 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Conserved Sequence | Crystallography | Drosophila | Drosophila Proteins | Humans | Insect Proteins | Molecular Sequence Data | Multigene Family | Protein Binding | Protein Structure, Tertiary | RNA, Messenger | RNA-Binding Proteins | Transcription Factors