SARS-CoV-2 Spike glycoprotein receptor-binding domain (RBD) in the "up" conformation (RBD)

The SARS-CoV-2 Spike glycoprotein receptor-binding domain (RBD) is a critical component of the S1 subunit of the spike protein, responsible for mediating the virus's entry into host cells (UniProt P0DTC2). In its "up" conformation, the RBD is accessible and capable of binding to the human Angiotensin-Converting Enzyme 2 (ACE2) receptor, a prerequisite for membrane fusion and infection (Wrapp et al., Science 2020). This specific conformational state is the primary target for the host's neutralizing antibody response and the focus of most therapeutic monoclonal antibodies and vaccine designs (NIH COVID-19 Treatment Guidelines). By binding to the RBD in the "up" position, drugs can sterically hinder the interaction with ACE2, effectively preventing the virus from attaching to and entering the cell. However, the RBD is highly prone to mutations, leading to the emergence of variants of concern that can evade existing treatments. Understanding the structural dynamics of the RBD "up" state is essential for developing broad-spectrum antivirals and next-generation vaccines.

Other names

Spike RBDS-RBDReceptor-binding domain of the S1 subunitSARS-CoV-2 S protein RBDRBD in the open conformationRBD in the up conformation

Neutralization of viral entry by competitively or sterically blocking the interaction between the viral receptor-binding domain and the host cell Angiotensin-Converting Enzyme 2 (ACE2) receptor.