Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2. Self-assembles into homopentamers. The capsid has an icosahedral symmetry and consists of 72 capsomers, with each capsomer being a pentamer of L1. Interacts with the minor capsid protein L2; this interaction is necessary for viral genome encapsidation. Interacts with protein E2; this interaction enhances E2-dependent replication and transcription activation (PubMed:25911730). Interacts with host KPNA2; this interaction mediates the nuclear localization of L1 capsomers (PubMed:11971900). Interacts with host ITGA6 (PubMed:11341777). Interacts with host SDC1; this interaction promotes efficient infection of keratinocytes (PubMed:26289843). ISGylated by host HERC5, this results in dominant-negative effect on virus infectivity. HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans. Belongs to the papillomaviridae L1 protein family. Icosahedral capsid structure