1ib2: Difference between revisions
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'''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN''' | '''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN''' | ||
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[[Category: Wang, X.]] | [[Category: Wang, X.]] | ||
[[Category: Zamore, P D.]] | [[Category: Zamore, P D.]] | ||
[[Category: | [[Category: Pumilio-homology domain,puf motif]] | ||
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Revision as of 16:47, 2 May 2008
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. 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 Fri May 2 19:47:37 2008
