Summary for 5GW6
| Entry DOI | 10.2210/pdb5gw6/pdb |
| Descriptor | Eukaryotic translation initiation factor 4E, GLYCEROL (3 entities in total) |
| Functional Keywords | cap-dependent, translation, cap-free |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm, P-body : P06730 |
| Total number of polymer chains | 1 |
| Total formula weight | 22979.91 |
| Authors | Brown, C.J. (deposition date: 2016-09-08, release date: 2016-10-19, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 27916520DOI: 10.1016/j.str.2016.11.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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