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Human adenoviruses are non‐enveloped, double stranded DNA viruses responsible for many upper‐respiratory infections and eye infections. It is composed of a spherical capsid that surrounds the viral genome. The trimeric fiber protein, exposed on the capsid exterior, is unique to adenoviruses and facilitates the attachment to the host cell via interactions between the knob domain and cell surface proteins. After entry into the host the virus is carried to the nucleus, where the capsid disassociates and the DNA passes through the nuclear pore. The adenovirus is of particular interest for the role it may play in targeted gene therapy as a vector.Further study of the virus' structure, specifically the knob domain located on the fiber protein, may allow for genetic alterations to specific cell surface proteins and to circumvent neutralizing antibodies. In addition, knowledge of the structural details provides ways to disrupt their assembly and disassembly, thereby interfering with their natural lifecycle and associated infections. The structural details can also be used to re‐target the adenoviruses to the cells of interest and deliver specific genes, thus making it a useful delivery vehicle. The El Capitan SMART (Students Modeling A Research Topic) Team modeled the fiber protein using 3D printing technology. Supported by a grant from the HHMI Pre‐College Program

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Viral infections are one of the leading causes of death in humans and are usually caused by the adenovirus. The early region protein (E1A) is a multifunctional protein expressed by the adenovirus and essential for transformation of the host cell, ultimately resulting in oncogenesis. Through E1A's interactions with the host cell's retinoblastoma protein (pRb) and CREB binding protein (CBP), E1A prevents natural cellular functions. Our focus is the interaction site between E1A and CBP/p300, specifically the transcriptional adaptor zinc finger‐2 (TAZ2) of CBP/p300. Upon interaction with the TAZ2 domain, E1A undergoes coupled folding, allowing it to bind with TAZ2, competing with, and inactivating, the transactivation domain (TAD) of the tumor suppressor p53. Through competition with p53, E1A is able to inhibit apoptosis and cell cycle arrest, thus causing the cell to divide uncontrollably. E1A has the ability to reprogram gene expression. Understanding the structure of the complex will help us to design a therapeutic that would prevent E1A from interacting with CBP, allowing normal interaction with p53 to occur. This will prevent cancer in association with adenovirus infection and help us to understand more about cancer‐causing viruses in general. The El Capitan High School SMART Team (Students Modeling A Research Topic) modeled E1A using 3D printing technology. Supported by a grant from HHMI Pre‐College Program