Source:http://linkedlifedata.com/resource/pubmed/id/11859078
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
2002-5-6
|
| pubmed:databankReference | |
| pubmed:abstractText |
Eukaryotic translation initiation factor 2alpha (eIF2alpha) is a member of the eIF2 heterotrimeric complex that binds and delivers Met-tRNA(i)(Met) to the 40 S ribosomal subunit in a GTP-dependent manner. Phosphorylation/dephosphorylation of eIF2alpha at Ser-51 is the major regulator of protein synthesis in eukaryotic cells. Here, we report the first structural analysis on eIF2, the three-dimensional structure of a 22-kDa N-terminal portion of human eIF2alpha by x-ray diffraction at 1.9 A resolution. This structure contains two major domains. The N terminus is a beta-barrel with five antiparallel beta-strands in an oligonucleotide binding domain (OB domain) fold. The phosphorylation site (Ser-51) is on the loop connecting beta3 and beta4 in the OB domain. A helical domain follows the OB domain, and the first helix has extensive interactions, including a disulfide bridge, to fix its orientation with respect to the OB domain. The two domains meet along a negatively charged groove with highly conserved residues, indicating a likely site for protein-protein interaction.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
10
|
| pubmed:volume |
277
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
17057-61
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:11859078-Amino Acid Sequence,
pubmed-meshheading:11859078-Animals,
pubmed-meshheading:11859078-Binding Sites,
pubmed-meshheading:11859078-Crystallography, X-Ray,
pubmed-meshheading:11859078-Disulfides,
pubmed-meshheading:11859078-Eukaryotic Initiation Factor-2,
pubmed-meshheading:11859078-Humans,
pubmed-meshheading:11859078-Models, Molecular,
pubmed-meshheading:11859078-Molecular Sequence Data,
pubmed-meshheading:11859078-Phosphorylation,
pubmed-meshheading:11859078-Protein Conformation,
pubmed-meshheading:11859078-Protein Structure, Secondary,
pubmed-meshheading:11859078-Protein Structure, Tertiary,
pubmed-meshheading:11859078-RNA, Transfer, Met,
pubmed-meshheading:11859078-Sequence Homology, Amino Acid,
pubmed-meshheading:11859078-Serine,
pubmed-meshheading:11859078-X-Ray Diffraction
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha.
|
| pubmed:affiliation |
Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, New York 14853-1301, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|