1m8z
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1m8z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8z, resolution 1.9Å" /> '''Crystal Structure Of...)
Next diff →
Revision as of 16:02, 12 November 2007
|
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
1M8Z is a Single protein structure of sequence from Homo sapiens with BME as ligand. This structure superseeds the now removed PDB entry 1IB3. 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
Page seeded by OCA on Mon Nov 12 18:08:56 2007
