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Introduction

Structure & Function

SARS-COV-2 Spike Protein

Structure And Function

The of SARS-COV-2 is a symmetric trimer featuring 3 spike glycoprotein chains (UNIPROT: P0DTC2). Each monomer of the spike is called a spike glycoprotein, and it contains 2 main parts: The S1 and S2 subunits^[3]. However, the native spike protein does not exist in this state prior to infection. The protein is actually inactive initially, but is later activated by proteases cleaving the inactive S protein into its two active subunits^[3]. The S1 subunit contains the N-Terminal domain (NTD), C-Terminal Domain (CRD), and the Receptor Binding Domain (RBD). The RBD is responsible for binding to the ACE2 receptor on the surface of the target cell, as well as neutralizing antibodies. The NTD, CTD, and their relevant interfaces actually play much larger roles in the binding of the spike protein to ACE2 than the RBD does due to their larger surface areas^[3]. The S2 subunit is responsible for viral fusion and entry. Once bound to ACE2, and after the different domains in S2 have anchored to the membrane as well as delivered the viral envelope, the the S2 subunit changes conformation from the pre-hairpin to postfusion-hairpin conformation^[3].

Figure 1. Spike protein shown in "B-Factor"; depicting mobility and flexibility of different portions. Depicted in red are the most mobile, whilst dark blue are the least mobile.

Throughout the entire process, the spike protein has 3 main conformations. An conformation; an active, "open" conformation; and a conformation mentioned previously^[3][4][5]. In the closed conformation, the RBDs of each monomer are tucked inwards, preventing interaction. In the open conformation, however, 1 or more of these RBDs can be in the "up" conformation, meaning they are exposed and able to interact within the extracellular space. Mainly, there exits a "" and "" conformation in this phase^[4][5]. Depicted in Figure 1, the RBDs of the spike protein have the highest mobility, which further support the many conformational changes in which they are involved.

Function

ACE2

Structure

Function

Minibinders

Structure

Function

Design

Implications

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