Hepatitis C Virus (HCV) has become a very prevalent disease affecting over 200million people worldwide. HCV amongst its various mechanisms of intrusion, enters the human cells by interaction with human CD81. The tetraspanin membrane protein CD81 interacts with envelope protein E2 of HCV. This helps viral entry into the host and facilitates further proliferation of the virus. Targeting this interaction could prove fruitful in eradicating the proliferation of the virus. We have insilico studied the interaction of E2 and CD81. Seventeen different sequences of E2 protein were homology modelled using 2ZCH_P - Chain P, Crystal Structure of Human Prostate Specific Antigen, as a template and using modeller 9v8 software. CD81 - E2 protein interaction was studied using Vakser Lab - GRAMM-X Protein-Protein Docking Web Server v.1.2.0. 170 models were generated, 10 each of a particular sequence. In almost all 17 protein models, residues cystine (2-6), Threonine (5-9) and Arginine (5-19) were found to be active in interactions with CD81.