NSP5

NSP5 is a nonstructural protein that is encoded by the SARS-CoV-2 virus. It is also known as 3C-like proteinase (3CLpro) or main protease (Mpro). NSP5 is crucial for the replication of the virus, making it a potential target for antiviral drugs.

Function[edit | edit source]

NSP5 is a cysteine protease that cleaves the polyproteins pp1a and pp1ab at 11 different sites. This results in the release of the virus's nonstructural proteins, which are necessary for the replication of the virus. NSP5 itself is released by the action of NSP4 and NSP6.

Structure[edit | edit source]

NSP5 is composed of three domains. The first two domains (I and II) form a chymotrypsin-like fold, while the third domain (III) is a globular cluster of five alpha helices. The active site of the enzyme is located in a cleft between domains I and II.

Inhibition[edit | edit source]

Due to its essential role in the life cycle of the virus, NSP5 is a target for antiviral drugs. Several inhibitors of NSP5 have been identified, including peptidomimetic compounds and Michael acceptor-based inhibitors.

See also[edit | edit source]

NSP5 Resources
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