Abstract 2141 Structural and functional explorations of the DNA-binding domains of the human transcription repressor capicua

The transcriptional repressor capicua (CIC) is a key protein in cellular and developmental processes, and whose mutation or improper regulation is associated with tumor progression and cancer metastasis. Previous research has shown that two subdomains of CIC, an HMG-box and a C1 domain, are required for physiological binding to an octameric consensus sequence, 5'-TGAATGAA-3'. Here, we report the crystal structure of the two CIC domains, connected by a minimal linker region, in complex with a consensus DNA oligomer in a 2.95-Å resolution crystal structure.

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Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109279
Primary Topic
DNA and Nucleic Acid Chemistry
Type
article
Field-Weighted Citation Impact
0.00

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Abstract 2141 Structural and functional explorations of the DNA-binding domains of the human transcription repressor capicua

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Abstract 2141 Structural and functional explorations of the DNA-binding domains of the human transcription repressor capicua

Daniel Dowling, Alexey Veraksa, Gerardo Jiménez, Jonathan K. Webb, Khandan Ilkhani, Marta Forés, Andrew Gnann, Jeremy Liew
article en

Abstract

The transcriptional repressor capicua (CIC) is a key protein in cellular and developmental processes, and whose mutation or improper regulation is associated with tumor progression and cancer metastasis. Previous research has shown that two subdomains of CIC, an HMG-box and a C1 domain, are required for physiological binding to an octameric consensus sequence, 5'-TGAATGAA-3'. Here, we report the crystal structure of the two CIC domains, connected by a minimal linker region, in complex with a consensus DNA oligomer in a 2.95-Å resolution crystal structure.

Journal of Biological ChemistryVol. 301(5)
University of Massachusetts Boston (US)
National Institutes of Health
Zero hunger
Openalex Percentile: Top 88%
DNA and Nucleic Acid Chemistry
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