1xly: Difference between revisions

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[[Image:1xly.gif|left|200px]]
{{Seed}}
[[Image:1xly.png|left|200px]]


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{{STRUCTURE_1xly|  PDB=1xly  |  SCENE=  }}  
{{STRUCTURE_1xly|  PDB=1xly  |  SCENE=  }}  


'''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p'''
===X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p===




==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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{{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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