|1ib2, resolution 1.90Å ()|
CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN
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.
Crystal structure of a Pumilio homology domain., Wang X, Zamore PD, Hall TM, Mol Cell. 2001 Apr;7(4):855-65. PMID:11336708
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Wang X, Zamore PD, Hall TM. Crystal structure of a Pumilio homology domain. Mol Cell. 2001 Apr;7(4):855-65. PMID:11336708