1wqs: Difference between revisions

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==Overview==

Norovirus 3C-like proteases are crucial to proteolytic processing of, norovirus polyproteins. We determined the crystal structure of the 3C-like, protease from Chiba virus, a norovirus, at 2.8-A resolution. An active, site including Cys139 and His30 is present, as is a hydrogen bond network, that stabilizes the active site conformation. In the oxyanion hole, backbone, a structural difference was observed probably upon substrate, binding. A peptide substrate/enzyme model shows that several interactions, between the two components are critical for substrate binding and that the, S1 and S2 sites appropriately accommodate the substrate P1 and P2, residues, respectively. Knowledge of the structure and a previous, mutagenesis study allow us to correlate proteolysis and structure.

Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.

==About this Structure==

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[[Category: oxyanion hole]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:11 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Norovirus 3C-like proteases are crucial to proteolytic processing of, norovirus polyproteins. We determined the crystal structure of the 3C-like, protease from Chiba virus, a norovirus, at 2.8-A resolution. An active, site including Cys139 and His30 is present, as is a hydrogen bond network, that stabilizes the active site conformation. In the oxyanion hole, backbone, a structural difference was observed probably upon substrate, binding. A peptide substrate/enzyme model shows that several interactions, between the two components are critical for substrate binding and that the, S1 and S2 sites appropriately accommodate the substrate P1 and P2, residues, respectively. Knowledge of the structure and a previous, mutagenesis study allow us to correlate proteolysis and structure.
+Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.
 ==About this Structure==
@@ Line 27: / Line 27: @@
 [[Category: oxyanion hole]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:42:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:11 2008''