author(s)
Pravas Ranjan Sahoo, Bijayendranath Mohanty, Swagat Mohapatra, Kamadev Sethy, Prakash Chandra Behera

abstract
The present study was conducted to know the detail functional aspects and molecular interaction of p53 tumor suppressor protein of Bos taurus at Department of Veterinary Biochemistry, College of Veterinary Science & AH, Bhubaneswar from time period between September 2017 to February 2018. The P53 tumor suppressor protein plays a central role in the prevention of cancer in bovine by participating in the signaling pathway of apoptosis that protect against unnatural cell growth. Thus, a functional analysis of this protein is required to know the various interactions with other proteins and to find the conserved domain in its structure, for the development of putative therapeutic targets against the tumor. So in this study, the amino acid sequence of the bovine p53 was retrieved from NCBI site, the protein protein interaction was done to analyze the functional behavior of this protein through search tool for the retrieval of interacting proteins (STRING) platform. The conserved domain was searched for this protein on pfam database. It was found there were eleven nodes and 32 edges in its network and having strong interaction with MDM2 and CREBBP with score 0.998 but posses weak interaction with CDKN2A with a score of 0.991.It was observed DNA-binding domain is the important conserved domain present in this protein with no co expression with other proteins in bos taurus.