1kl9
From Proteopedia
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- | [[Image:1kl9.jpg|left|200px]] | + | [[Image:1kl9.jpg|left|200px]] |
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- | '''Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha''' | + | {{Structure |
+ | |PDB= 1kl9 |SIZE=350|CAPTION= <scene name='initialview01'>1kl9</scene>, resolution 1.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1KL9 is a [ | + | 1KL9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KL9 OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha., Nonato MC, Widom J, Clardy J, J Biol Chem. 2002 May 10;277(19):17057-61. Epub 2002 Feb 21. PMID:[http:// | + | Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha., Nonato MC, Widom J, Clardy J, J Biol Chem. 2002 May 10;277(19):17057-61. Epub 2002 Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11859078 11859078] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ob fold]] | [[Category: ob fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:18:58 2008'' |
Revision as of 10:18, 20 March 2008
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, resolution 1.90Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha
Contents |
Overview
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.
Disease
Known disease associated with this structure: Wolcott-Rallison syndrome OMIM:[604032]
About this Structure
1KL9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha., Nonato MC, Widom J, Clardy J, J Biol Chem. 2002 May 10;277(19):17057-61. Epub 2002 Feb 21. PMID:11859078
Page seeded by OCA on Thu Mar 20 12:18:58 2008
Categories: Homo sapiens | Single protein | Clardy, J. | Nonato, M C. | Widom, J. | ZN | Helical domain | Ob fold