We all are aware of the covid-19 pandemic since last year it spread worldwide. New information is being published regularly regarding SARS-CoV-2. Recently, a comparative study is published showing the structural and functional details of the interactions of SARS-CoV-2 spike glycoproteins and angiotensin enzyme -2 (ACE-2) receptor [1].

The authors of this paper analyzed the interactions between SARS-CoV-2 and ACE-2 receptors using bioinformatics approaches. According to this study [1],

• the binding affinity of SARS-CoV-2 (− 6 kcal mol⁻¹) with the ACE-2 receptor is higher than that of SARS-CoV (− 2 kcal mol⁻¹).
• this increased binding affinity may be due to the mutations that occurred at three critical points found out by the authors.
• these three mutations include Asn479Gln, Pro462Ala, and Leu472Phe.
• the mutated region includes the receptor-binding domain of spike glycoprotein.
• the MM-PBSA binding analysis of SARS-CoV, SARS-CoV-2, and the chimeric structure bound to ACE-2 revealed the lowest binding energy of SARS-CoV-2 (− 31.5759 ± 2.4425).
• mutations including Pro462Ala and Leu472Phe in SARS-CoV-2 altered the binding affinity.
• Pro462Ala mutation helps in making the end of the loop present in SARS-CoV-2 flexible and thereby, facilitates the binding of the SARS-CoV-2 to its receptor.
• according to the results, Lys31 in the ACE-2 receptor is involved in its interaction with the N-terminal and middle regions of the receptor-binding motif.

For more information, read here.

---

References

1. Jafary, F., Jafari, S. & Ganjalikhany, M.R. (2021). In silico investigation of critical binding pattern in SARS-CoV-2 spike protein with angiotensin-converting enzyme 2. Sci Rep 11, 6927.