Ligand-specific changes in conformational flexibility mediate long-range allostery in the lac repressor

Biological regulation ubiquitously depends on protein allostery, but the regulatory mechanisms are incompletely understood, especially in proteins that undergo ligand-induced allostery with few structural changes. Here we used hydrogen-deuterium exchange with mass spectrometry (HDX/MS) to map allost...

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Detalles Bibliográficos
Autores principales: Glasgow, Anum, Hobbs, Helen T., Perry, Zion R., Wells, Malcolm L., Marqusee, Susan, Kortemme, Tanja
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9977783/
https://www.ncbi.nlm.nih.gov/pubmed/36859492
http://dx.doi.org/10.1038/s41467-023-36798-1

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9977783/
https://www.ncbi.nlm.nih.gov/pubmed/36859492
http://dx.doi.org/10.1038/s41467-023-36798-1

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