1m8x
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(New page: 200px<br /> <applet load="1m8x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8x, resolution 2.20Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:02, 12 November 2007
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CRYSTAL STRUCTURE OF THE PUMILIO-HOMOLOGY DOMAIN FROM HUMAN PUMILIO1 IN COMPLEX WITH NRE1-14 RNA
Overview
Puf proteins are developmental regulators that control mRNA stability and, translation by binding sequences in the 3' untranslated regions of their, target mRNAs. We have determined the structure of the RNA binding domain, of the human Puf protein, Pumilio1, bound to a high-affinity RNA ligand., The RNA binds the concave surface of the molecule, where each of the, protein's eight repeats makes contacts with a different RNA base via three, amino acid side chains at conserved positions. We have mutated these three, side chains in one repeat, thereby altering the sequence specificity of, Pumilio1. Thus, the high affinity and specificity of the PUM-HD for RNA is, achieved using multiple copies of a simple repeated motif.
About this Structure
1M8X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Modular recognition of RNA by a human pumilio-homology domain., Wang X, McLachlan J, Zamore PD, Hall TM, Cell. 2002 Aug 23;110(4):501-12. PMID:12202039
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