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| {{STRUCTURE_1kl9| PDB=1kl9 | SCENE= }} | | {{STRUCTURE_1kl9| PDB=1kl9 | SCENE= }} |
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| '''Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha'''
| | ===Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11859078}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11859078 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11859078}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Helical domain]] | | [[Category: Helical domain]] |
| [[Category: Ob fold]] | | [[Category: Ob fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:52:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:30:15 2008'' |