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New Information regarding binding pattern of SARS-CoV-2 and ACE-2

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sars-cov-2 & ace-2 receptor

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.

Tariq is founder of Bioinformatics Review and CEO at IQL Technologies. His areas of expertise include algorithm design, phylogenetics, MicroArray, Plant Systematics, and genome data analysis. If you have questions, reach out to him via his homepage.

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