Impact of P278A mutation conferring Breast Cancer susceptibility in the p53 DNA-Binding Core Domain interacting partners. Yeguvapalli Suneetha, Chitrala Kumaraswamy Naidu. Department of zoology, Sri venkateswara University, Tirupati, India.

   Breast cancer is the second most common cancer faced by the women around the world. Both genetic and non genetic factors constitute risk for breast cancer. Several studies have showed that TP53 constitute a high risk factor to Breast Cancer [1, 2]. TP53 is known to interact with several proteins [3]. Among the several domains present in TP53 DNA binding core domain is known to show interaction with Hypoxia inducible factor-1 alpha (HIF-1a), Heat shock protein 90 (Hsp90), Rad51, 53BP2/ASPP2 and Bcl-XL/Bak protein [4]. In our previous study, we have analyzed the deleterious phenotypic effect conferring to breast cancer by rs17849781 (P278A) and further we have analyzed the structural effect of the P278A mutation on the p53 DNA-binding core domain[5]. In the present study, we aim at analyzing the impact of P278A on p53 DNA-binding core domain interacting partners using computational approaches. Key words: Computational analysis, Protein-Protein interactions, Breast Cancer, TP53, Deleterious mutations References: 1.Mavaddat N, Antoniou AC, Easton DF, Garcia-Closas M: Genetic susceptibility to breast cancer. Mol Oncol 2010, 4:174-191. 2.Gasco M, Shami S, Crook T: The p53 pathway in breast cancer. Breast Cancer Res 2002, 4:70-76. 3.Keller DM, Zeng SX, Lu H: Interaction of p53 with cellular proteins. Methods Mol Biol 2003, 234:121-133. 4.Fernandez-Fernandez MR, Sot B: The relevance of protein-protein interactions for p53 function: the CPE contribution. Protein Eng Des Sel 2011, 24:41-51. 5.Y Suneetha, Naidu CK: Structural effect of P278A mutation conferring breast cancer susceptibility in the p53 DNA-binding core domain. BMC Proceedings 2012, 6:P50.