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X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2pX-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSelective 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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