For the past five decades, acquired immunodeficiency syndrome has been the cause of a salient global epidemic. The unavailability of an effective vaccine has been a colossal hurdle in combating the disease. To develop an efficacious treatment, it is vital to inspect the mechanism of the virus and the host cell interactions. The causative agent, the human immunodeficiency virus, targets the CD4 receptor harbouring cells. Interactions of cells with the viral spikes, gp120, trigger conformational changes, prompting viral attachment. Upon further inspection, the role of coreceptor is evident. Chemokine co-receptor 5 is the predominant co-receptor utilized by the virus and interaction with the variable loop 3 crown, allows binding and subsequent fusion of the virus with the membrane of the host cell. The ~13 residue long V3 crown possesses a highly conserved GPGR/Q motif thus serves as an excellent epitope. To utilize it as the drug target, it is necessary to have a detailed understanding of the V3 crown structure. Using NMR spectroscopy, the spatial arrangement of the protons in the V3 crown sequence in an unbound and bound state with the TZM-bl cells was studied. A promising outcome was obtained as several protons in the V3 crown sequence showed spatial rearrangement when bound to CCR5. This serves as the foundation to decipher its three-dimensional structure when bound to the co-receptor which can serve as a remarkable contribution towards drug development.