SARS-CoV-2 enzyme Hel: Difference between revisions
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Nsp13 comprises of five domains: The N-terminal Zinc binding domain (ZBD) (amino acids 1-100), the stalk domain (101-150), 1B (151-261), 1A (262-442), and the 2A domain (443-601). The last three have been shown to be responsible for nucleic acid binding and the NTPase activity, while the ZBD and 1A can directly interact with nsp12 to enhance the helicase activity of nsp13. Together they fold in a triangular shape with 1A, 1B and 2A forming the base and the stalk domain and ZBD at the apex<ref name="Romano"/>. Nsp13 might form a stable holo-RdRp complex with [[SARS-CoV-2 enzyme RdRp|nsp12]], [[SARS-CoV-2 protein NSP7|nsp7]] and [[SARS-CoV-2 protein NSP8|nsp8]] by interacting with the nsp8 extensions and the nsp12 thumb domain and may play a role in backtracking<ref name="Chen"/>. | Nsp13 comprises of five domains: The N-terminal Zinc binding domain (ZBD) (amino acids 1-100), the stalk domain (101-150), 1B (151-261), 1A (262-442), and the 2A domain (443-601). The last three have been shown to be responsible for nucleic acid binding and the NTPase activity, while the ZBD and 1A can directly interact with nsp12 to enhance the helicase activity of nsp13. Together they fold in a triangular shape with 1A, 1B and 2A forming the base and the stalk domain and ZBD at the apex<ref name="Romano"/>. Nsp13 might form a stable holo-RdRp complex with [[SARS-CoV-2 enzyme RdRp|nsp12]], [[SARS-CoV-2 protein NSP7|nsp7]] and [[SARS-CoV-2 protein NSP8|nsp8]] by interacting with the nsp8 extensions and the nsp12 thumb domain and may play a role in backtracking<ref name="Chen"/>. | ||
== See also == | == See also == | ||