5GW6

Water-Bridge Mediates Recognition of mRNA Cap in eIF4E

「5ABI」から置き換えられました

5GW6 の概要

• エントリーDOI: 10.2210/pdb5gw6/pdb
• 分子名称: Eukaryotic translation initiation factor 4E, GLYCEROL (3 entities in total)
• 機能のキーワード: cap-dependent, translation, cap-free
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, P-body : P06730
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22979.91

構造登録者

Brown, C.J. (登録日: 2016-09-08, 公開日: 2016-10-19, 最終更新日: 2023-11-08)

主引用文献

Lama, D.,Pradhan, M.R.,Brown, C.J.,Eapen, R.S.,Joseph, T.L.,Kwoh, C.K.,Lane, D.P.,Verma, C.S.
Water-Bridge Mediates Recognition of mRNA Cap in eIF4E
Structure, 25:188-194, 2017

PubMed Abstract: Ligand binding pockets in proteins contain water molecules, which play important roles in modulating protein-ligand interactions. Available crystallographic data for the 5' mRNA cap-binding pocket of the translation initiation factor protein eIF4E shows several structurally conserved waters, which also persist in molecular dynamics simulations. These waters engage an intricate hydrogen-bond network between the cap and protein. Two crystallographic waters in the cleft of the pocket show a high degree of conservation and bridge two residues, which are part of an evolutionarily conserved scaffold. This appears to be a preformed recognition module for the cap with the two structural waters facilitating an efficient interaction. This is also recapitulated in a new crystal structure of the apo protein. These findings open new windows for the design and screening of compounds targeting eIF4E.

PubMed: 27916520
DOI: 10.1016/j.str.2016.11.006

実験手法

X-RAY DIFFRACTION (1.97 Å)