Author: Akisawa, K.; Hatada, R.; Okuwaki, K.; Kitahara, S.; Tachino, Y.; Mochizuki, Y.; Komeiji, Y.; Tanaka, S.
Title: Fragment molecular orbital based interaction analyses on complexes between SARS-CoV-2 RBD variants and ACE2 Cord-id: 4hosl9b9 Document date: 2021_1_1
ID: 4hosl9b9
Snippet: The SARS-CoV-2 virus initiates infection of human cells by recognizing the human angiotensin-converting enzyme 2 (ACE2) with the receptor binding domain (RBD) of the viral spike protein. Thus, the variant of concern (VOC) with mutations on RBD is of special interest. Here, we present a series of interaction analyses for the RBD-ACE2 complex of the wild-type (PDB ID: 6M0J) and those of B.1.1.7 (alpha), B.1.351 (beta) and P.1 (gamma) VOCs, based on the fragment molecular orbital (FMO) calculations
Document: The SARS-CoV-2 virus initiates infection of human cells by recognizing the human angiotensin-converting enzyme 2 (ACE2) with the receptor binding domain (RBD) of the viral spike protein. Thus, the variant of concern (VOC) with mutations on RBD is of special interest. Here, we present a series of interaction analyses for the RBD-ACE2 complex of the wild-type (PDB ID: 6M0J) and those of B.1.1.7 (alpha), B.1.351 (beta) and P.1 (gamma) VOCs, based on the fragment molecular orbital (FMO) calculations. The results revealed that the RBD variants have a higher affinity for ACE2 than the wild type does.
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