Protein-Folding Chaperones Predict Structure-Function Relationships and Cancer Risk in BRCA1 Mutation Carriers

Published: 28 February 2024| Version 3 | DOI: 10.17632/rmj7fwm6n7.3
Contributors:
,
,
,
, Georgios Karras

Description

We used a high-throughput LUMIER assay to test whether the binding patterns of protein-folding chaperones can be used to predict structure-function relationships of BRCA1 variants and the clinical manifestations of BRCA1 mutations in carriers. Our findings are presented in the following tables. Table S1. Chaperone binding detects BRCA1-BRCT pathogenic ClinVar variants and rationally designed variants that disrupt domain structure Table S2. Computational analysis of thermodynamic stability for pathogenic BRCA1-BRCT missense mutations in ClinVar Table S3. Diverse functional outcomes of BRCA1-BRCT variants detected by chaperone binding Table S4. Features of human hypomorphic BRCA1 variants characterized by chaperones Table S5. Human BRCA1 carriers exhibiting early disease onset identified by chaperone binding

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Institutions

University of Texas MD Anderson Cancer Center

Categories

Breast Cancer, Protein-Protein Interaction, Protein Structure Prediction, BRCA1 Protein, Allele

Funding

NCI

K22CA222938

Cancer Prevention and Research Institute of Texas

RR180005

NCI

F32CA253780

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