Abstract
Hereditary breast cancer constitutes 5–10% of all breast cancer cases. Inherited mutations in the BRCA1 and BRCA2 tumor-suppressor genes account for the majority of hereditary breast cancer cases. The BRCA1 C-terminal region (BRCT) has a functional duplicated globular domain, which helps with DNA damage repair and cell cycle checkpoint protein control. More than 100 distinct BRCA1 missense variants with structural and functional effects have been documented within the BRCT domain. Interpreting the results of mutation screening of tumor-suppressor genes that can have high-risk susceptibility mutations is increasingly important in clinical practice. This study includes a novel mutation, p.His1746 Pro (c.5237A>C), which was found in BRCA1 exon 20 of a breast cancer patient. In silico analysis suggests that this mutation could alter the stability and orientation of the BRCT domain and the differential binding of the BACH1 substrate.
Highlights
Breast cancer is the most common neoplastic disease in women
The mutation found in codon 1746 at nucleotide c.5237A>C (CAC CCC) has not yet been reported, as evidenced by the Human Genome Variation Society (HGVS) or Breast Cancer Information Core (BIC)
Several missense mutations reported in BRCA1 C-terminal region (BRCT) repeats of the breast cancer gene one (BRCA1) gene are responsible for the malfunction of tumor-suppressor activity, as evidenced from several clinical reports
Summary
Breast cancer is the most common neoplastic disease in women. It is significantly influenced by hereditary factors. The mutations in the tumor-suppressor BRCA1 gene are associated with hereditary breast cancer [8, 9]. The BRCT domain seems to function as a protein-protein interacting moiety and directly recognizes the phosphorylated Ser 990 site of BACH1. The significance of these interactions provides clues to the molecular basis that underlies cellcycle regulation and DNA repair [13]. This report provides mutation analysis of the BRCA1 gene of a special case with novel mutation and functional effect using an in silico and docking study
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