Selected article for: "binding domain and cryo em"
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_7
    Snippet: Human coronavirus spike (S) proteins are molecular complexes each formed by three protein chains [3] , [14] - [16] . To better understand S protein structure [3] , we started by studying the protomer, the structural unit of the trimeric complex, and compared the protomer structure of the current SARS-CoV-2 with protomers of previously identified human coronaviruses, including SARS-CoV-1 [15] , MERS-CoV [16] , and HCoV-HKU1 [14] . We modeled each .....
    Document: Human coronavirus spike (S) proteins are molecular complexes each formed by three protein chains [3] , [14] - [16] . To better understand S protein structure [3] , we started by studying the protomer, the structural unit of the trimeric complex, and compared the protomer structure of the current SARS-CoV-2 with protomers of previously identified human coronaviruses, including SARS-CoV-1 [15] , MERS-CoV [16] , and HCoV-HKU1 [14] . We modeled each protomer system from the corresponding cryo-EM S protein structure (see Methods for more details). There are three major structural domains which constitute the protomer: the amino-terminal domain (NTD), receptor binding domain (RBD), and the S2 domain.

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