User:Dora Bonadio/Sandbox 1: Difference between revisions

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== SARS-CoV-2 main protease (M<sup>pro</sup>)==

The Mpro protease (also known as 3CLpro), is a viral non structural protein from the virus SARS-CoV-2 (1), responsible for a major outbreak of the disease called COVID-19, declared pandemic by WHO in 11 march 2020 (2). It has an important role in virus replication, as it’s responsible for cleavage of the polyproteins of the virus, alongside with papain-like protease(s) (3).

The Mpro protease (also known as 3CLpro), is a viral non structural protein from the virus SARS-CoV-2 <ref name="Crystal_structure">PMID:32198291</ref>(1), responsible for a major outbreak of the disease called COVID-19, declared pandemic by WHO in 11 march 2020 (2). It has an important role in virus replication, as it’s responsible for cleavage of the polyproteins of the virus, alongside with papain-like protease(s) (3).

==Your Heading Here (maybe something like 'Structure')==

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== Function ==

The Mpro protein function is mainly deduced from the function of SARS-CoV virus Mpro , which has a 96% amino acid identity and a highly similar three-dimensional structure with SARS-CoV-2 Mpro <ref~~>PMID:32198291<~~/~~ref~~>. As a protease, Mpro is an enzyme that causes proteolysis, which means that it breaks protein peptide bonds by hydrolysis (4). Indeed, the Mpro processes the replicase polyprotein 1ab (pp1ab ~790 kDa) translated from the viral RNA ORF1ab <ref>PMID:32198291</ref>(1, 5). In fact, Mpro cleaves 11 sites of pp1ab and the recognition sequence at most sites is between Leu-Gln and (Ser, Ala, Gly) (1, 3). Proteins resulting from this polyprotein cleavage are non-structural proteins (NSPs) and they seem to contribute with viral replication and transcription (5). Thus, by processing an important number of non-structural proteins, this enzyme plays a critical role in SARS-CoV-2 replication.

The Mpro protein function is mainly deduced from the function of SARS-CoV virus Mpro , which has a 96% amino acid identity and a highly similar three-dimensional structure with SARS-CoV-2 Mpro <ref name="Crystal_structure" />. As a protease, Mpro is an enzyme that causes proteolysis, which means that it breaks protein peptide bonds by hydrolysis (4). Indeed, the Mpro processes the replicase polyprotein 1ab (pp1ab ~790 kDa) translated from the viral RNA ORF1ab <ref>PMID:32198291</ref>(1, 5). In fact, Mpro cleaves 11 sites of pp1ab and the recognition sequence at most sites is between Leu-Gln and (Ser, Ala, Gly) (1, 3). Proteins resulting from this polyprotein cleavage are non-structural proteins (NSPs) and they seem to contribute with viral replication and transcription (5). Thus, by processing an important number of non-structural proteins, this enzyme plays a critical role in SARS-CoV-2 replication.

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 ==<!-- Your Heading Here --> SARS-CoV-2 main protease (M<sup>pro</sup>)==
-The Mpro protease (also known as 3CLpro), is a viral non structural protein from the virus SARS-CoV-2 (1), responsible for a major outbreak of the disease called COVID-19, declared pandemic by WHO in 11 march 2020 (2). It has an important role in virus replication, as it’s responsible for cleavage of the polyproteins of the virus, alongside with papain-like protease(s) (3).
+The Mpro protease (also known as 3CLpro), is a viral non structural protein from the virus SARS-CoV-2 <ref name="Crystal_structure">PMID:32198291</ref>(1), responsible for a major outbreak of the disease called COVID-19, declared pandemic by WHO in 11 march 2020 (2). It has an important role in virus replication, as it’s responsible for cleavage of the polyproteins of the virus, alongside with papain-like protease(s) (3).
 ==Your Heading Here (maybe something like 'Structure')==
@@ Line 15: / Line 15: @@
 == Function ==
-The Mpro protein function is mainly deduced from the function of SARS-CoV virus Mpro , which has a 96% amino acid identity and a highly similar three-dimensional structure with SARS-CoV-2 Mpro <ref>PMID:32198291</ref>. As a protease, Mpro is an enzyme that causes proteolysis, which means that it breaks protein peptide bonds by hydrolysis (4). Indeed, the Mpro processes the replicase polyprotein 1ab (pp1ab ~790 kDa) translated from the viral RNA ORF1ab <ref>PMID:32198291</ref>(1, 5). In fact, Mpro cleaves 11 sites of pp1ab and the recognition sequence at most sites is between Leu-Gln and (Ser, Ala, Gly) (1, 3). Proteins resulting from this polyprotein cleavage are non-structural proteins (NSPs) and they seem to contribute with viral replication and transcription (5). Thus, by processing an important number of non-structural proteins, this enzyme plays a critical role in SARS-CoV-2 replication.
+The Mpro protein function is mainly deduced from the function of SARS-CoV virus Mpro , which has a 96% amino acid identity and a highly similar three-dimensional structure with SARS-CoV-2 Mpro <ref name="Crystal_structure" />. As a protease, Mpro is an enzyme that causes proteolysis, which means that it breaks protein peptide bonds by hydrolysis (4). Indeed, the Mpro processes the replicase polyprotein 1ab (pp1ab ~790 kDa) translated from the viral RNA ORF1ab <ref>PMID:32198291</ref>(1, 5). In fact, Mpro cleaves 11 sites of pp1ab and the recognition sequence at most sites is between Leu-Gln and (Ser, Ala, Gly) (1, 3). Proteins resulting from this polyprotein cleavage are non-structural proteins (NSPs) and they seem to contribute with viral replication and transcription (5). Thus, by processing an important number of non-structural proteins, this enzyme plays a critical role in SARS-CoV-2 replication.