Receptor-binding domain of spike glycoprotein S1 subunit (RBD (Receptor-binding domain))

The receptor-binding domain (RBD) of the spike glycoprotein S1 subunit is a critical region of the SARS-CoV-2 spike protein responsible for attachment to the host cell receptor angiotensin-converting enzyme 2 (ACE2), directly mediating viral entry[3][7]. The S1 subunit (residues 14–685) includes the RBD, which specifically recognizes ACE2 and undergoes conformational changes to expose or hide the binding interface[1][3][7]. The RBD is a twisted five-stranded antiparallel β-sheet with a receptor-binding motif insertion, forming the main interface for ACE2 interaction[7]. This domain is the principal target for neutralizing antibodies, vaccines, and entry inhibitors and determines host specificity, pathogenicity, and immune evasion. Mutations in the RBD can impact transmissibility and resistance to antibody-based therapeutics. The RBD is one of the most actively studied viral protein domains in the context of COVID-19 prevention, diagnostics, and treatment[2][3][5][6][7].

Other names

Spike protein receptor-binding domainSARS-CoV-2 RBDS1-RBDSpike RBDCOVID-19 spike RBD

Blockade of RBD-ACE2 interaction, preventing viral entry (antibodies and clinical drugs). Induction of neutralizing antibodies after vaccination or passive administration. Some drugs stabilize the spike protein at a non-fusogenic state.