Abstract
A vast majority of the ovarian and the breast cancers are sporadic and result from the accumulation of genetic damage. Most preclinical data suggest that women experiencing ovarian cancer are prone to breast cancer and vice versa. Similar domains and similar binding sites often imply similar protein?protein interactions and similar functions. Zinc finger of P53 and Ring finger of BRCA1 are similar domains having mostly binding activity. BRCT domain of BRCA1 is helpful in DNA-damage repair and cell cycle checkpoint functioning. This study sets out to check similar pattern, domain and residue-specific mutation, which may interact with expressions of P53 and BRCA1.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
BRCA1 Protein / chemistry
-
BRCA1 Protein / genetics*
-
BRCA1 Protein / metabolism*
-
Breast Neoplasms / genetics*
-
Breast Neoplasms / metabolism*
-
Computational Biology / methods
-
DNA, Neoplasm / genetics
-
DNA, Neoplasm / metabolism
-
Female
-
Genes, BRCA1
-
Genes, p53
-
Humans
-
Models, Molecular
-
Molecular Sequence Data
-
Mutant Proteins / genetics
-
Mutant Proteins / metabolism
-
Mutation
-
Ovarian Neoplasms / genetics*
-
Ovarian Neoplasms / metabolism*
-
Protein Interaction Domains and Motifs
-
Protein Structure, Tertiary
-
Sequence Alignment / statistics & numerical data
-
Tumor Suppressor Protein p53 / chemistry
-
Tumor Suppressor Protein p53 / genetics*
-
Tumor Suppressor Protein p53 / metabolism*
-
Zinc Fingers
Substances
-
BRCA1 Protein
-
BRCA1 protein, human
-
DNA, Neoplasm
-
Mutant Proteins
-
TP53 protein, human
-
Tumor Suppressor Protein p53