1xly
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(New page: 200px<br /><applet load="1xly" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xly, resolution 1.95Å" /> '''X-RAY STRUCTURE OF T...)
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Revision as of 04:02, 21 November 2007
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X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p
Overview
Selective transport of mRNAs in ribonucleoprotein particles (mRNP) ensures, asymmetric distribution of information within and among eukaryotic cells., Actin-dependent transport of ASH1 mRNA in yeast represents one of the, best-characterized examples of mRNP translocation. Formation of the ASH1, mRNP requires recognition of zip code elements by the RNA binding protein, She2p. We determined the X-ray structure of She2p at 1.95 A resolution., She2p is a member of a previously unknown class of nucleic acid binding, proteins, composed of a single globular domain with a five alpha helix, bundle that forms a symmetric homodimer. After demonstrating potent, dimer-dependent RNA binding in vitro, we mapped the RNA binding surface of, She2p to a basic helical hairpin in vitro and in vivo and present a, mechanism for mRNA-dependent initiation of ASH1 mRNP complex assembly.
About this Structure
1XLY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
She2p is a novel RNA binding protein with a basic helical hairpin motif., Niessing D, Huttelmaier S, Zenklusen D, Singer RH, Burley SK, Cell. 2004 Nov 12;119(4):491-502. PMID:15537539
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