Mutations to transcription factor MAX allosterically increase DNA selectivity by altering folding and binding pathways
Abstract Understanding how proteins discriminate between preferred and non-preferred ligands (‘selectivity’) is essential for predicting biological function and a central goal of protein engineering efforts, yet the biophysical mechanisms underpinning selectivity remain poorly understood. Towards th...
Saved in:
Main Authors: | Renee Hastings, Arjun K. Aditham, Nicole DelRosso, Peter H. Suzuki, Polly M. Fordyce |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2025-01-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-024-55672-2 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Fragment Screening Identifies Novel Allosteric Binders and Binding Sites in the VHR (DUSP3) Phosphatase
by: Jiaqian Wu, et al.
Published: (2025-01-01) -
Allosteric coupling between G‐protein binding and extracellular ligand binding sites in GPR52 revealed by 19F‐NMR and cryo‐electron microscopy
by: Yanliu Fan, et al.
Published: (2023-04-01) -
Identifying Allosteric Small-Molecule Binding Sites of Inactive NS2B-NS3 Proteases of Pathogenic <i>Flaviviridae</i>
by: Hovakim Grabski, et al.
Published: (2024-12-01) -
Discovery of potent allosteric antibodies inhibiting EGFR
by: Léxane Fournier, et al.
Published: (2024-12-01) -
Enhancing NMDA Receptor Function: Recent Progress on Allosteric Modulators
by: Lulu Yao, et al.
Published: (2017-01-01)