1xly

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[[Image:1xly.gif|left|200px]]
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{{STRUCTURE_1xly| PDB=1xly | SCENE= }}
{{STRUCTURE_1xly| PDB=1xly | SCENE= }}
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'''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p'''
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===X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15537539 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15537539}}
==About this Structure==
==About this Structure==
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[[Category: Five helix bundle]]
[[Category: Five helix bundle]]
[[Category: Rna-binding protein]]
[[Category: Rna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:11:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:17:34 2008''

Revision as of 04:17, 28 July 2008

Image:1xly.png

Template:STRUCTURE 1xly

X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p

Template:ABSTRACT PUBMED 15537539

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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