1xk5: Difference between revisions

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[[Image:1xk5.gif|left|200px]]
{{Seed}}
[[Image:1xk5.png|left|200px]]


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{{STRUCTURE_1xk5|  PDB=1xk5  |  SCENE=  }}  
{{STRUCTURE_1xk5|  PDB=1xk5  |  SCENE=  }}  


'''Crystal structure of the m3G-cap-binding domain of snurportin1 in complex with a m3GpppG-cap dinucleotide'''
===Crystal structure of the m3G-cap-binding domain of snurportin1 in complex with a m3GpppG-cap dinucleotide===




==Overview==
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In higher eukaryotes the biogenesis of spliceosomal UsnRNPs involves a nucleocytoplasmic shuttling cycle. After the m7G-cap-dependent export of the snRNAs U1, U2, U4 and U5 to the cytoplasm, each of these snRNAs associates with seven Sm proteins. Subsequently, the m7G-cap is hypermethylated to the 2,2,7-trimethylguanosine (m3G)-cap. The import adaptor snurportin1 recognises the m3G-cap and facilitates the nuclear import of the UsnRNPs by binding to importin-beta. Here we report the crystal structure of the m3G-cap-binding domain of snurportin1 with bound m3GpppG at 2.4 A resolution, revealing a structural similarity to the mRNA-guanyly-transferase. Snurportin1 binds both the hypermethylated cap and the first nucleotide of the RNA in a stacked conformation. This binding mode differs significantly from that of the m7G-cap-binding proteins Cap-binding protein 20 (CBP20), eukaryotic initiation factor 4E (eIF4E) and viral protein 39 (VP39). The specificity of the m3G-cap recognition by snurportin1 was evaluated by fluorescence spectroscopy, demonstrating the importance of a highly solvent exposed tryptophan for the discrimination of m7G-capped RNAs. The critical role of this tryptophan and as well of a tryptophan continuing the RNA base stack was confirmed by nuclear import assays and cap-binding activity tests using several snurportin1 mutants.
The line below this paragraph, {{ABSTRACT_PUBMED_15920472}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15920472}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1., Strasser A, Dickmanns A, Luhrmann R, Ficner R, EMBO J. 2005 Jul 6;24(13):2235-43. Epub 2005 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15920472 15920472]
Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1., Strasser A, Dickmanns A, Luhrmann R, Ficner R, EMBO J. 2005 Jul 6;24(13):2235-43. Epub 2005 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15920472 15920472]
Purification, crystallization and preliminary crystallographic data of the m3G cap-binding domain of human snRNP import factor snurportin 1., Strasser A, Dickmanns A, Schmidt U, Penka E, Urlaub H, Sekine M, Luhrmann R, Ficner R, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1628-31. Epub 2004, Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15333938 15333938]
Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure., Huber J, Cronshagen U, Kadokura M, Marshallsay C, Wada T, Sekine M, Luhrmann R, EMBO J. 1998 Jul 15;17(14):4114-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9670026 9670026]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Strasser, A.]]
[[Category: Strasser, A.]]
[[Category: Protein-rna-complex]]
[[Category: Protein-rna-complex]]
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