
Summary
p38 MAPK is a fascinating class of molecules crucial for various cellular functions such as cellular proliferation and apoptosis, and is implicated in many pathologies. Various bioinformatics tools have been employed to investigate the biological role and sequence analysis of p38 MAPK. Four paralogues of p38 MAPK exist in humans and comparison of paralogues with five other species suggest p38 MAPK exhibits evolutionary conservation. FASTA and BLASTA were used to analyse the primary structure of these paralogues, demonstrating high similarity of the amino acid sequences between the different species, and supporting the hypothesis p38 MAPK function has been conserved over time. Multiple sequence alignment was used to determine conserved domains amongst species, postulating the ATP binding site, KIM docking site, activation loop and active site function have been conserved. The tertiary (3D) structure of p38 MAPK was determined using RasMol in order to further explore the functions of the various modular domains of p38 MAPK. The structural and functional analysis of p38 MAPK is pivotal to medical research in the hope treatments against pathologies involving p38 MAPK can be developed.