Sandbox Reserved 324: Difference between revisions
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{{STRUCTURE_1q8k| PDB=1q8k | SCENE= }} | {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }} | ||
=Structure= | =Structure= | ||
The human eIF2 structure was determined by NMR spectroscopy<ref name="1q8k"/>. The human eIF2 structure is a small structure made of two domains<ref name="1q8k"/>. These two domains have a unique characteristic in that they are mobile relative to the other domain<ref name="1q8k"/>. The N | |||
The human eIF2 structure was determined by NMR spectroscopy<ref name="1q8k"/>. The human eIF2 structure is a small structure made of two domains<ref name="1q8k"/>. These two domains have a unique characteristic in that they are mobile relative to the other domain<ref name="1q8k"/>. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years<ref name="dhal">doi:10.1016<ref/>, 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 similarity in sequence between the two<ref name="1q8k"/>. | |||
=Function= | =Function= | ||
Revision as of 09:34, 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)
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].
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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 | ||||||||
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<ref name="dhal">doi:10.1016Cite error: The opening <ref> tag is malformed or has a bad name, 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 similarity in sequence between the two[1].