(376af) Molecular Dynamics Simulation on Human Beta-Defensin Type 3 Binding with CXCR4 Receptor | AIChE

(376af) Molecular Dynamics Simulation on Human Beta-Defensin Type 3 Binding with CXCR4 Receptor

Authors 

Penfield, J. - Presenter, Tennessee Technological University
The protein human beta-defensin type 3 (hBD-3) is a component of the human innate immune system, mainly secreted from human epithelial tissues and mucosa. It is known to have multiple roles, including bactericide, binding with chemokine receptors (notably CXCR4), and is involved in the inhibition of HIV-1 replication. Structural changes can modify the chemotactic activities of hBD-3. Many factors govern its structure, especially its six cysteine residues that are capable of forming three pairs of disulfide bonds. The molecular detail of hBD-3’s diverse chemotactic function is not yet known. All-atom molecular dynamics simulations using NAMD software were performed on hBD-3 analogs of varying structures interacting with the CXCR4 receptor embedded inside lipid bilayers. The binding structure and dynamics of hBD-3 with the CXCR4 receptor will be studied, and the result may aid in understanding the relationship between hBD-3’s structure and its chemotactic functions.