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='''Human eIF2 (1q8k)'''= | ='''Human eIF2 (1q8k)'''= | ||
{{STRUCTURE_1q8k| PDB=1q8k | SCENE= | {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default/1}} | ||
=Introduction= | =Introduction= | ||
Revision as of 21:44, 28 March 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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Human eIF2 (1q8k)Human eIF2 (1q8k)
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| 1q8k, 15 NMR models () | |||||||||
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| Gene: | EIF2S1 OR EIF2A (Homo sapiens) | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
IntroductionIntroduction
The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNAmeti and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 [1].
StructureStructure
The human eIF2 structure was determined by NMR spectroscopy[1]. The human eIF2 structure is a small structure made of two domains[1]. These two domains have a unique characteristic in that they are mobile relative to the other domain[1]. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years[2], where the C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two[1].
FunctionFunction
ReferencesReferences
- ↑ 1.0 1.1 1.2 1.3 1.4 Ito T, Marintchev A, Wagner G. Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure. 2004 Sep;12(9):1693-704. PMID:15341733 doi:10.1016/j.str.2004.07.010
- ↑ Daniel Zaidman, Paul Gehrtz, Mihajlo Filep, Daren Fearon, Ronen Gabizon, Alice Douangamath, Jaime Prilusky, Shirly Duberstein, Galit Cohen, C. David Owen, Efrat Resnick, Claire Strain-Damerell, Petra Lukacik, Haim Barr, Martin A. Walsh, Frank von Delft, Nir London, An automatic pipeline for the design of irreversible derivatives identifies a potent SARS-CoV-2 Mpro inhibitor, Cell Chemical Biology, 2021 doi:https://dx.doi.org/10.1016/j.chembiol.2021.05.018