1ib2
From Proteopedia
CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN
Structural highlights
FunctionPUM1_HUMAN Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPuf 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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