Sandbox Reserved 324

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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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-tRNA^meti and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 .

spinqualitylabelsall models PDB ID 1q8k Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1q8k, 15 NMR models ()
Gene:	EIF2S1 OR EIF2A (Homo sapiens)
Structural annotation: Resources: CATH : 1Q8Ka02, 1Q8Ka01, 1Q8Ka03 InterPro : Ipr011488, Ipr003029, Ipr012340 Pfam : PF00575, PF07541 SCOP : d1q8ka1, d1q8ka2 UniProt : P05198
Functional annotation: Cellular component: cytoplasm polysome nucleus eukaryotic translation initiation factor 2 complex eukaryotic translation initiation factor 2B complex Biological process: translation regulation of translational initiation in response to stress regulation of translation Molecular function: RNA binding protein binding translation initiation factor activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

StructureStructure

The human eIF2 structure was determined by NMR spectroscopy. The human eIF2 structure is a small structure made of two domains. These two domains have a unique characteristic in that they are mobile relative to the other domain. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years<ref name="dhal">doi:10.1016, 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.