Author: Renhong Yan; Yuanyuan Zhang; Yingying Guo; Lu Xia; Qiang Zhou
Title: Structural basis for the recognition of the 2019-nCoV by human ACE2 Document date: 2020_2_20
ID: elo7kfun_15
Snippet: Structures of ACE2 in complex with nCoV-RBD and SARS-RBD establish the molecular basis to dissect their different affinities. In this study, we carefully analyzed the interface in both RBD-ACE2 complexes. Whereas some of the variations may strengthen the interactions between nCoV-RBD and ACE2, others may reduce the affinity compared to that between SARS-RBD and ACE2. For instance, the change from Val404 to Lys317 may result in tighter association.....
Document: Structures of ACE2 in complex with nCoV-RBD and SARS-RBD establish the molecular basis to dissect their different affinities. In this study, we carefully analyzed the interface in both RBD-ACE2 complexes. Whereas some of the variations may strengthen the interactions between nCoV-RBD and ACE2, others may reduce the affinity compared to that between SARS-RBD and ACE2. For instance, the change from Val404 to Lys317 may result in tighter association because of the salt bridge formation between Lys317 and Asp30 of ACE2 (Figs. 3C, 4C) . Change of Leu472 to Phe486 may also make stronger van der Waals contact with Met82 (Fig. 4D) .
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