2LLX

Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1

2LLX の概要

• エントリーDOI: 10.2210/pdb2llx/pdb
• 関連するPDBエントリー: 1DT9 2HST 2KTU 2KTV 3E1Y
• NMR情報: BMRB: 18092
• 分子名称: Eukaryotic peptide chain release factor subunit 1 (1 entity in total)
• 機能のキーワード: protein synthesis termination, stop codon recognition, translation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P62495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16769.35

構造登録者

Polshakov, V.I.,Eliseev, B.D.,Birdsall, B.,Frolova, L.Y. (登録日: 2011-11-18, 公開日: 2012-05-30, 最終更新日: 2024-05-15)

主引用文献

Polshakov, V.I.,Eliseev, B.D.,Birdsall, B.,Frolova, L.Y.
Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.
Protein Sci., 21:896-903, 2012

PubMed Abstract: The high-resolution NMR structure of the N-domain of human eRF1, responsible for stop codon recognition, has been determined in solution. The overall fold of the protein is the same as that found in the crystal structure. However, the structures of several loops, including those participating in stop codon decoding, are different. Analysis of the NMR relaxation data reveals that most of the regions with the highest structural discrepancy between the solution and solid states undergo internal motions on the ps-ns and ms time scales. The NMR data show that the N-domain of human eRF1 exists in two conformational states. The distribution of the residues having the largest chemical shift differences between the two forms indicates that helices α2 and α3, with the NIKS loop between them, can switch their orientation relative to the β-core of the protein. Such structural plasticity may be essential for stop codon recognition by human eRF1.

PubMed: 22517631
DOI: 10.1002/pro.2067

実験手法

SOLUTION NMR