Crystal structure of the HMGA AT-hook 1 domain bound to the minor groove of AT-rich DNA and inhibition by antikinetoplastid drugs

Crystal structure of the HMGA AT-hook 1 domain bound to the minor groove of AT-rich DNA and inhibition by antikinetoplastid drugs

Abstract High mobility group (HMG) proteins are intrinsically disordered nuclear non-histone chromosomal proteins that play an essential role in many biological processes by regulating the expression of numerous genes in eukaryote cells. HMGA proteins contain three DNA binding motifs, the “AT-hooks”...

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Bibliographic Details
Main Authors: J. Jonathan Nué-Martinez, Marta Maturana, Laura Lagartera, Juan-Antonio Rodríguez-Gutiérrez, Roeland Boer, J. Lourdes Campos, Núria Saperas, Christophe Dardonville
Format: Article
Language:English
Published: Nature Portfolio 2024-10-01
Series:Scientific Reports
Subjects:
High mobility group (HMG) protein
HMGA AT-hook 1 domain
AT-hook 1 binding inhibitor
DNA minor groove binder
kinetoplastid parasite
crystal structure.
Online Access:https://doi.org/10.1038/s41598-024-77522-3
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https://doi.org/10.1038/s41598-024-77522-3

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