5OA3
Human 40S-eIF2D-re-initiation complex
5OA3 の概要
| エントリーDOI | 10.2210/pdb5oa3/pdb |
| EMDBエントリー | 3770 |
| 分子名称 | Eukaryotic translation initiation factor 2D, 40S ribosomal protein S5, 40S ribosomal protein S6, ... (39 entities in total) |
| 機能のキーワード | translation re-initiation complex, small ribosomal subunit, rna binding protein, eukaryotic translation initiation factor, translation |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 38 |
| 化学式量合計 | 1389584.97 |
| 構造登録者 | Weisser, M.,Schaefer, T.,Leibundgut, M.,Boehringer, D.,Aylett, C.H.S.,Ban, N. (登録日: 2017-06-20, 公開日: 2017-08-09, 最終更新日: 2024-05-15) |
| 主引用文献 | Weisser, M.,Schafer, T.,Leibundgut, M.,Bohringer, D.,Aylett, C.H.S.,Ban, N. Structural and Functional Insights into Human Re-initiation Complexes. Mol. Cell, 67:447-456.e7, 2017 Cited by PubMed Abstract: After having translated short upstream open reading frames, ribosomes can re-initiate translation on the same mRNA. This process, referred to as re-initiation, controls the translation of a large fraction of mammalian cellular mRNAs, many of which are important in cancer. Key ribosomal binding proteins involved in re-initiation are the eukaryotic translation initiation factor 2D (eIF2D) or the homologous complex of MCT-1/DENR. We determined the structures of these factors bound to the human 40S ribosomal subunit in complex with initiator tRNA positioned on an mRNA start codon in the P-site using a combination of cryoelectron microscopy and X-ray crystallography. The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA. PubMed: 28732596DOI: 10.1016/j.molcel.2017.06.032 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.2 Å) |
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