AIDS is a major worldwide epidemic caused by human immunodeficiency virus (HIV). In 2007, there were 33 million people living with HIV/AIDS. A protein in the HIV envelope, gp120 recognizes CD4, a protein found on the surface of human T cells. Binding of gp120 to CD4 enables HIV to attach and gain access to the cell. Neutralizing antibodies with broad reactivity to HIV have been identified. One such antibody, IgG1 b12, binds the CD4‐binding site of gp120, blocking CD4 attachment. Antibody b12 comprises two identical heavy chains and two identical light chains held together by disulfide bonds, forming a Y. The chains have constant and variable regions. The tip of each arm contains an antigen binding site (Fab), allowing the antibody to bind specifically to a particular antigen. The base of the antibody (Fc region) is made up of two heavy chains. Flexible hinges connect Fab arms to the Fc allowing conformation changes. A finger‐like projection extending above the surface of the antigen binding site allows it to fit into the recessed binding site of gp120. The Governor's Academy SMART (Students Modeling a Research Topic) team, in collaboration with MSOE, designed a model using 3D printing technology to highlight the structural features of b12. Understanding its structure and the nature of its interaction with gp120 may allow development of an effective vaccine against HIV‐1. Supported by a grant from theNIH‐NCRR‐SEPA
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