User:Dora Bonadio/Sandbox 1: Difference between revisions

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== Structure ==

The Mpro is a protein of approximately 30 kDa <ref name="replication" /><ref name="ofmpro">Jin, Zhenming, Xiaoyu Du, Yechun Xu, Yongqiang Deng, Meiqin Liu, Yao Zhao, Bing Zhang, et al. 2020. ‘Structure of M pro from SARS-CoV-2 and Discovery of Its Inhibitors’. Nature, April, 1–5. https://doi.org/10.1038/s41586-020-2223-y. </ref> consisting of <scene name='84/845941/Assembly/3'>two protomers</scene> containing 306 amino acid residues each <ref name="Crystal_structure" />. This protomers dimerize forming a homodimer <ref name="Crystal_structure" />. Each protomer consists of <scene name='84/845941/Domains/1'>three domains</scene>: I (<scene name='84/845941/Domaini/1'>chymotrypsin-like</scene>; residues 10-99), II (<scene name='84/845941/Domainii/1'>picornavirus 3C protease-like</scene>; residues 100-182), and III (a globular cluster; residues 198-303). Domains I and II comprise six-stranded antiparallel β-barrels and domain III comprises five α-helices <ref name="Crystal_structure" /><ref name="ofmpro" />. The substrate-binding site is located between domains I and II with the catalytic site containing the amino acid residues Cys145 and His41 <ref name="Crystal_structure" />. Domain III, in turn, has been shown to be involved in the regulation of Mpro dimerization, what is necessary for the catalytic activity of this enzyme once it helps to shape the substrate-binding site <ref name="Crystal_structure" /><ref name="reveals"> PMID:12093723</ref>.

The Mpro is a protein of approximately 30 kDa <ref name="replication" /><ref name="ofmpro">Jin, Zhenming, Xiaoyu Du, Yechun Xu, Yongqiang Deng, Meiqin Liu, Yao Zhao, Bing Zhang, et al. 2020. ‘Structure of M pro from SARS-CoV-2 and Discovery of Its Inhibitors’. Nature, April, 1–5. https://doi.org/10.1038/s41586-020-2223-y. </ref> consisting of <scene name='84/845941/Assembly/3'>two protomers</scene> containing 306 amino acid residues each <ref name="Crystal_structure" />. This protomers dimerize forming a homodimer <ref name="Crystal_structure" />. Each protomer consists of <scene name='84/845941/Domains/1'>three domains</scene>: I (<scene name='84/845941/Domaini/1'>chymotrypsin-like</scene>; residues 10-99), II (<scene name='84/845941/Domainii/2'>picornavirus 3C protease-like</scene>; residues 100-182), and III (a globular cluster; residues 198-303). Domains I and II comprise six-stranded antiparallel β-barrels and domain III comprises five α-helices <ref name="Crystal_structure" /><ref name="ofmpro" />. The substrate-binding site is located between domains I and II with the catalytic site containing the amino acid residues Cys145 and His41 <ref name="Crystal_structure" />. Domain III, in turn, has been shown to be involved in the regulation of Mpro dimerization, what is necessary for the catalytic activity of this enzyme once it helps to shape the substrate-binding site <ref name="Crystal_structure" /><ref name="reveals"> PMID:12093723</ref>.

== An attractive drug target ==

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 == Structure ==
-The Mpro is a protein of approximately 30 kDa <ref name="replication" /><ref name="ofmpro">Jin, Zhenming, Xiaoyu Du, Yechun Xu, Yongqiang Deng, Meiqin Liu, Yao Zhao, Bing Zhang, et al. 2020. ‘Structure of M pro from SARS-CoV-2 and Discovery of Its Inhibitors’. Nature, April, 1–5. https://doi.org/10.1038/s41586-020-2223-y. </ref> consisting of <scene name='84/845941/Assembly/3'>two protomers</scene> containing 306 amino acid residues each <ref name="Crystal_structure" />. This protomers dimerize forming a homodimer <ref name="Crystal_structure" />. Each protomer consists of <scene name='84/845941/Domains/1'>three domains</scene>: I (<scene name='84/845941/Domaini/1'>chymotrypsin-like</scene>; residues 10-99), II (<scene name='84/845941/Domainii/1'>picornavirus 3C protease-like</scene>; residues 100-182), and III (a globular cluster; residues 198-303). Domains I and II comprise six-stranded antiparallel β-barrels and domain III comprises five α-helices <ref name="Crystal_structure" /><ref name="ofmpro" />. The substrate-binding site is located between domains I and II with the catalytic site containing the amino acid residues Cys145 and His41 <ref name="Crystal_structure" />. Domain III, in turn, has been shown to be involved in the regulation of Mpro dimerization, what is necessary for the catalytic activity of this enzyme once it helps to shape the substrate-binding site <ref name="Crystal_structure" /><ref name="reveals"> PMID:12093723</ref>.
+The Mpro is a protein of approximately 30 kDa <ref name="replication" /><ref name="ofmpro">Jin, Zhenming, Xiaoyu Du, Yechun Xu, Yongqiang Deng, Meiqin Liu, Yao Zhao, Bing Zhang, et al. 2020. ‘Structure of M pro from SARS-CoV-2 and Discovery of Its Inhibitors’. Nature, April, 1–5. https://doi.org/10.1038/s41586-020-2223-y. </ref> consisting of <scene name='84/845941/Assembly/3'>two protomers</scene> containing 306 amino acid residues each <ref name="Crystal_structure" />. This protomers dimerize forming a homodimer <ref name="Crystal_structure" />. Each protomer consists of <scene name='84/845941/Domains/1'>three domains</scene>: I (<scene name='84/845941/Domaini/1'>chymotrypsin-like</scene>; residues 10-99), II (<scene name='84/845941/Domainii/2'>picornavirus 3C protease-like</scene>; residues 100-182), and III (a globular cluster; residues 198-303). Domains I and II comprise six-stranded antiparallel β-barrels and domain III comprises five α-helices <ref name="Crystal_structure" /><ref name="ofmpro" />. The substrate-binding site is located between domains I and II with the catalytic site containing the amino acid residues Cys145 and His41 <ref name="Crystal_structure" />. Domain III, in turn, has been shown to be involved in the regulation of Mpro dimerization, what is necessary for the catalytic activity of this enzyme once it helps to shape the substrate-binding site <ref name="Crystal_structure" /><ref name="reveals"> PMID:12093723</ref>.
 == An attractive drug target ==