Identifying interactions between TDP-43's N-terminal and RNA-binding domains.

ABSTRACT: TAR DNA-binding Protein 43 kilodaltons (TDP-43) plays a crucial role in the pathophysiology and progression of amyotrophic lateral sclerosis, affecting familial and sporadic cases. TDP-43 is an intrinsically disordered multidomain protein that consists of an N-terminal domain (NTD_1-102), two tandem RNA recognition motifs (RRM1_102-177 and RRM2_191-260), and an intrinsically disordered glycine-rich C-terminal_261-414 domain. We previously identified a chemical probe that led to allosteric alterations between the RRM and NTD of TDP-43. We attributed these changes to potential interdomain interactions between the NTD and RRM segments. In this work, we compared the 2D [¹H,¹⁵N] HSQC-NMR resonances of two constructs, TDP-43_102-2

SUBMITTER: Scott DD 

PROVIDER: S-EPMC12442443 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature