1ib2
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(New page: 200px<br /> <applet load="1ib2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ib2, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:22, 12 November 2007
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CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN
Overview
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.
About this Structure
1IB2 is a Single protein structure of sequence from Homo sapiens with BME as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a Pumilio homology domain., Wang X, Zamore PD, Hall TM, Mol Cell. 2001 Apr;7(4):855-65. PMID:11336708
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