title: Functional assessment of intrinsic disorder central domains of BRCA1.
abstract: The most studied function of BRCA1 is that of tumor suppression through its role in DNA repair and transcription regulation. Germline mutations discovered in a larger cohort of patients, abrogate BRCA1 interactions with reported cellular partners, and are responsible for breast and ovarian cancer. The different functional regions of BRCA1 interact with nearly 30 different cellular partners. Thus, it becomes clinically significant to understand the detailed protein-protein interactions associated with functional regions of BRCA1. Different overlapping central domains of BRCA1 have been characterized using in silico, in vitro and biophysical approaches. To our conclusions, it has been observed that central domains of BRCA1 are intrinsically disordered and has large hydrodynamic radius with random coil like structures.
authors.affiliation: a Tata Memorial Centre, Advanced Centre for Treatment, Research and Education in Cancer , Kharghar , Navi Mumbai , Maharashtra 410 210 , India.
authors.forename: Lumbini R
authors.initials: LR
authors.lastname: Yadav
authors.affiliation: a Tata Memorial Centre, Advanced Centre for Treatment, Research and Education in Cancer , Kharghar , Navi Mumbai , Maharashtra 410 210 , India.
authors.forename: Sharad
authors.initials: S
authors.lastname: Rai
authors.affiliation: a Tata Memorial Centre, Advanced Centre for Treatment, Research and Education in Cancer , Kharghar , Navi Mumbai , Maharashtra 410 210 , India.
authors.forename: M V
authors.initials: MV
authors.lastname: Hosur
authors.affiliation: a Tata Memorial Centre, Advanced Centre for Treatment, Research and Education in Cancer , Kharghar , Navi Mumbai , Maharashtra 410 210 , India.
authors.forename: Ashok K
authors.initials: AK
authors.lastname: Varma
mesh_terms: D019313:BRCA1 Protein / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
chemical_list: D019313:BRCA1 Protein; D064267:Intrinsically Disordered Proteins; D008024:Ligands
keywords: BRCA1 central domains; intrinsic disorder; protein-protein interactions