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13629 Ensembl ENSG00000167658 ENSMUSG00000034994 UniProt P13639 P58252 RefSeq (mRNA) NM_001961 NM_007907 RefSeq (protein) NP_001952 NP_031933 Location (UCSC) Chr 19: 3.98 – 3.99 Mb Chr 10: 81.01 – 81.02 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene. It is the archaeal and eukaryotic ...
Elongation factors Bacterial Eukaryotic/Archaeal Function EF-Tu: eEF-1A (α) [2] mediates the entry of the aminoacyl tRNA into a free site of the ribosome. [4] EF-Ts: eEF-1B (β γ) [2] serves as the guanine nucleotide exchange factor for EF-Tu, catalyzing the release of GDP from EF-Tu. [2] EF-G: eEF-2
eEF-2 kinase is a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links multiple up-stream signals to the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 ( EEF2 ) and thus inhibits the EEF2 function.
Eukaryotic elongation factor 2 (eEF2) is a regulateable GTP-dependent translocase that moves nascent polypeptide chains from the A-site to the P-site in the ribosome. Phosphorylation of threonine 56 is inhibitory to the binding of eEF2 to the ribosome. [ 11 ]
It inhibits protein synthesis in the host cell through ADP-ribosylation of the eukaryotic elongation factor 2 (eEF2), which is an essential component for protein synthesis. It is slightly unusual in that it combines the A and B parts in the same protein chain: the pre-toxin is cleaved into two parts, then the two parts are joined by a disulfide ...
Eukaryotic Initiation Factor 2 (eIF2) is an eukaryotic initiation factor.It is required for most forms of eukaryotic translation initiation. eIF2 mediates the binding of tRNA i Met to the ribosome in a GTP-dependent manner. eIF2 is a heterotrimer consisting of an alpha (also called subunit 1, EIF2S1), a beta (subunit 2, EIF2S2), and a gamma (subunit 3, EIF2S3) subunit.
The only known physiological substrate of eEF-2K is eEF-2. Phosphorylation of eEF-2 at Thr-56 by eEF-2K leads to inhibition of the elongation phase of protein synthesis. Phosphorylation of Thr-56 is thought to reduce the affinity of eEF-2 for the ribosome, thereby slowing down the overall rate of elongation. [1]
The C domain blocks protein synthesis by transfer of ADP-ribose from NAD to a diphthamide residue of eukaryotic elongation factor 2 (eEF-2). [7] [3] A central translocation domain, known as the T domain or TM domain, has a multi-helical globin-like fold with two additional helices at the amino terminus but no counterpart to the first globin helix.