Extracellular receptors convey specific signals to the nucleus for modulation of gene expression through signaling molecules present in the cytoplasm. RIP1 is a signaling molecule involved in the proximal end of TNFα signaling. Signal transduction pathways involving RIP1 and JNK/p38 MAPKs are essential in inflammation and hence this signaling pathway serve as a target for novel drug development in inflammation mediated disorders. Though, the role of RIP1 in p38 MAPK activation have been reported before, the exact role of this signaling molecule in p38 MAPK activation is not clear. In silico prediction of RIP1 binding with p38 MAPK suggests a domain with amino acids 71-79 is involved in the interaction. Deletion of 71-79 amino acids in RIP1 destabilizes the interaction with p38 MAPK. This prediction if confirmed with wet lab analysis, can serve as a target for designing novel drugs for treating various disorders.