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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-2-22
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pubmed:databankReference |
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pubmed:abstractText |
Hu proteins bind to adenosine-uridine (AU)-rich elements (AREs) in the 3' untranslated regions of many short-lived mRNAs, thereby stabilizing them. Here we report the crystal structures of the first two RNA recognition motif (RRM) domains of the HuD protein in complex with an 11-nucleotide fragment of a class I ARE (the c-fos ARE; to 1.8 A), and with an 11-nucleotide fragment of a class II ARE (the tumor necrosis factor alpha ARE; to 2.3 A). These structures reveal a consensus RNA recognition sequence that suggests a preference for pyrimidine-rich sequences and a requirement for a central uracil residue in the clustered AUUUA repeats found in class II AREs. Comparison to structures of other RRM domain-nucleic acid complexes reveals two base recognition pockets in all the structures that interact with bases using residues in conserved ribonucleoprotein motifs and at the C-terminal ends of RRM domains. Different conformations of nucleic acid can be bound by RRM domains by using different combinations of base recognition pockets and multiple RRM domains.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ELAVL4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hu Paraneoplastic...,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fos,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sxl protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-5
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:11175903-AT Rich Sequence,
pubmed-meshheading:11175903-Amino Acid Sequence,
pubmed-meshheading:11175903-Binding Sites,
pubmed-meshheading:11175903-Consensus Sequence,
pubmed-meshheading:11175903-Crystallography, X-Ray,
pubmed-meshheading:11175903-Drosophila Proteins,
pubmed-meshheading:11175903-Hu Paraneoplastic Encephalomyelitis Antigens,
pubmed-meshheading:11175903-Humans,
pubmed-meshheading:11175903-Models, Molecular,
pubmed-meshheading:11175903-Molecular Sequence Data,
pubmed-meshheading:11175903-Nerve Tissue Proteins,
pubmed-meshheading:11175903-Protein Binding,
pubmed-meshheading:11175903-Protein Structure, Tertiary,
pubmed-meshheading:11175903-Proto-Oncogene Proteins c-fos,
pubmed-meshheading:11175903-RNA, Messenger,
pubmed-meshheading:11175903-RNA Stability,
pubmed-meshheading:11175903-RNA-Binding Proteins,
pubmed-meshheading:11175903-Response Elements,
pubmed-meshheading:11175903-Sequence Alignment,
pubmed-meshheading:11175903-Substrate Specificity,
pubmed-meshheading:11175903-Tumor Necrosis Factor-alpha
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pubmed:year |
2001
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pubmed:articleTitle |
Structural basis for recognition of AU-rich element RNA by the HuD protein.
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pubmed:affiliation |
Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA.
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pubmed:publicationType |
Journal Article
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