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Article

A BTB extension and ion-binding domain contribute to the pentameric structure and TFAP2A binding of KCTD1.

Structure (London, England : 1993) - 3 Oct 2024

Pinkas Daniel M, Bufton Joshua C, Hunt Alice E, Manning Charlotte E, Richardson William, Bullock Alex N

Abstract excerpt

KCTD family proteins typically assemble into cullin-RING E3 ligases. KCTD1 is an atypical member that functions instead as a transcriptional repressor. Mutations in KCTD1 cause developmental abnormalities and kidney fibrosis in scalp-ear-nipple syndrome. Here, we present unexpected mechanistic insights from the structure of human KCTD1. Disease-causing mutation P20S maps to an unrecognized extension of the BTB...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 39191250
DOI: 10.1016/j.str.2024.07.023
PMCID: PMC7618933

Genes

KCTD1
TFAP2A

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

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A BTB extension and ion-binding domain contribute to the pentameric structure and TFAP2A binding of KCTD1.PMID 39191250Read ↗

A BTB extension and ion-binding domain contribute to the pentameric structure and TFAP2A binding of KCTD1Semantic proximity Read ↗

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