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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-1-10
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pubmed:databankReference |
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pubmed:abstractText |
Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that recognizes and degrades aberrant mRNAs containing premature stop codons. A critical protein in NMD is Upf1p, which belongs to the helicase super family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to promote transitions in the structure of RNA or RNA-protein complexes. The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural comparison combined with mutational analysis identifies a likely single-stranded RNA (ssRNA)-binding channel, and a cycle of conformational change coupled to ATP binding and hydrolysis. These conformational changes alter the likely ssRNA-binding channel in a manner that can explain how ATP binding destabilizes ssRNA binding to Upf1p.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17159905-10199404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17159905-10999600,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17159905-9757107
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
253-64
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pubmed:dateRevised |
2011-1-5
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pubmed:meshHeading |
pubmed-meshheading:17159905-Adenosine Diphosphate,
pubmed-meshheading:17159905-Adenosine Triphosphate,
pubmed-meshheading:17159905-Allosteric Site,
pubmed-meshheading:17159905-Binding Sites,
pubmed-meshheading:17159905-Codon,
pubmed-meshheading:17159905-Crystallography, X-Ray,
pubmed-meshheading:17159905-Humans,
pubmed-meshheading:17159905-Hydrolysis,
pubmed-meshheading:17159905-Models, Molecular,
pubmed-meshheading:17159905-Molecular Conformation,
pubmed-meshheading:17159905-Nucleotides,
pubmed-meshheading:17159905-Protein Binding,
pubmed-meshheading:17159905-Protein Conformation,
pubmed-meshheading:17159905-Protein Structure, Tertiary,
pubmed-meshheading:17159905-Trans-Activators
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pubmed:year |
2007
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pubmed:articleTitle |
Structural and functional insights into the human Upf1 helicase core.
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pubmed:affiliation |
Laboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, Singapore, Singapore.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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