FoxP3 can fold into two distinct dimerization states with divergent functional implications for T cell homeostasis

Abstract excerpt

FoxP3 is an essential transcription factor (TF) for immunologic homeostasis, but how it utilizes the common forkhead DNA-binding domain (DBD) to perform its unique function remains poorly understood. We here demonstrate that, unlike other known forkhead TFs, FoxP3 forms a head-to-head dimer using a unique linker (Runx1-binding region, RBR) preceding the forkhead domain. Head-to-head dimerization confers distinct D...

Topics

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• Forkhead Transcription Factors
• Models, Molecular
• NFATC Transcription Factors
• Protein Multimerization
• Protein Structure, Quaternary
• Protein Structure, Tertiary
• Sequence Alignment
• T-Lymphocytes, Regulatory

Identifiers and source

Literature Corpus work

a9b53aa8-a21e-581c-a2d2-c581e15a4684

DOI

10.1101/2022.02.08.479534