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Article

Structural and functional divergence of cancer hotspot mutations in CREBBP.

Proceedings of the National Academy of Sciences of the United States of America - 29 Sept 2026

Zhang Wenchao, Yang Haopeng, Mechaly Ariel, Li Zhongyang, Cui Guiling, Regad Leslie, Duval Romain, Dairou Julien, Haouz Ahmed, Green Michael R, Rodrigues Lima Fernando

Abstract excerpt

CREBBP is among the most frequently mutated genes in human cancer and encodes a lysine acetyltransferase (KAT) protein that acetylates histones and nonhistone proteins to drive transcriptional activation. Mutations of CREBBP most frequently result in missense changes affecting the active site within the KAT domain. However, there has not yet been comprehensive biochemical, structural, and functional studies to...

Read the complete abstract on PubMed

Topics

CREB-Binding Protein
Humans
Mutation
Histones
Neoplasms
Acetylation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Models, Molecular

Acetyl Coenzyme A

Catalytic Domain

Protein Binding

Arginine

Source

Open in PubMed Open full text

Identifiers

PMID: 42771512
DOI: 10.1073/pnas.2605702123
PMCID: PMC13624666

Genes

CREBBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 2026.

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