Author: Serena H. Chen; M. Todd Young; John Gounley; Christopher Stanley; Debsindhu Bhowmik
Title: Distinct Structural Flexibility within SARS-CoV-2 Spike Protein Reveals Potential Therapeutic Targets Document date: 2020_4_18
ID: klb8oe9q_3
Snippet: understanding of the molecular pathways of SARS-CoV-2 and constituent structures. The structural biology community has made rapid progress towards this goal by experimentally determining several SARS-CoV-2 proteins, including the spike (S) [3] - [6] , nucleocapsid (N) [7] , and main protease (M pro ) [8] . The S protein is particularly important since it resides on the viral envelope and is responsible for host cell entry by engaging angiotensin-.....
Document: understanding of the molecular pathways of SARS-CoV-2 and constituent structures. The structural biology community has made rapid progress towards this goal by experimentally determining several SARS-CoV-2 proteins, including the spike (S) [3] - [6] , nucleocapsid (N) [7] , and main protease (M pro ) [8] . The S protein is particularly important since it resides on the viral envelope and is responsible for host cell entry by engaging angiotensin-converting enzyme 2 (ACE2) receptors [2] , [9] , [10] . Recent experimental structures of the SARS-CoV-2 S protein receptor binding domain (RBD) in complex with ACE2 provide detailed interface information [4] , [6] ; targeting this interface represents an active area of research for therapeutic development [11] . However, there may exist potential targets on the S protein besides the RBD domain.
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