Water-Bridge Mediates Recognition of mRNA Cap in eIF4E
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 a...
Saved in:
Main Authors: | Lama, Dilraj, Pradhan, Mohan R., Brown, Christopher J., Eapen, Rohan S., Joseph, Thomas L., Kwoh, Chee-Keong, Lane, David P., Verma, Chandra Shekhar |
---|---|
Other Authors: | School of Computer Science and Engineering |
Format: | Article |
Language: | English |
Published: |
2017
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/84992 http://hdl.handle.net/10220/42071 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
Similar Items
-
Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F complex
by: Frosi, Yuri, et al.
Published: (2023) -
Non-coding functions of alternative pre-mRNA splicing in development
by: Mockenhaupt, Stefan, et al.
Published: (2016) -
Non-coding functions of alternative pre-mRNA splicing in development
by: Mockenhaupt, Stefan, et al.
Published: (2015) -
Improved eIF4E binding peptides by phage display guided design : plasticity of interacting surfaces yield collective effects
by: Zhou, Weizhuang., et al.
Published: (2013) -
Structural insights reveal a recognition feature for tailoring hydrocarbon stapled-peptides against the eukaryotic translation initiation factor 4E protein
by: Lama, Dilraj, et al.
Published: (2019)