2hwk: Difference between revisions

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==Overview==

Alphavirus replication and propagation is dependent on the protease, activity of the viral nsP2 protein, which cleaves the nsP1234 polyprotein, replication complex into functional components. Thus, nsP2 is an, attractive target for drug discovery efforts to combat highly pathogenic, alphaviruses. Unfortunately, antiviral development has been hampered by a, lack of structural information for the nsP2 protease. Here, we report the, crystal structure of the nsP2 protease (nsP2pro) from Venezuelan equine, encephalitis alphavirus determined at 2.45 A resolution. The protease, structure consists of two distinct domains. The nsP2pro N-terminal domain, contains the catalytic dyad cysteine and histidine residues organized in a, protein fold that differs significantly from any known cysteine protease, or protein folds. The nsP2pro C-terminal domain displays structural, similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and, provides essential elements that contribute to substrate recognition and, may also regulate the structure of the substrate binding cleft.

Alphavirus replication and propagation is dependent on the protease activity of the viral nsP2 protein, which cleaves the nsP1234 polyprotein replication complex into functional components. Thus, nsP2 is an attractive target for drug discovery efforts to combat highly pathogenic alphaviruses. Unfortunately, antiviral development has been hampered by a lack of structural information for the nsP2 protease. Here, we report the crystal structure of the nsP2 protease (nsP2pro) from Venezuelan equine encephalitis alphavirus determined at 2.45 A resolution. The protease structure consists of two distinct domains. The nsP2pro N-terminal domain contains the catalytic dyad cysteine and histidine residues organized in a protein fold that differs significantly from any known cysteine protease or protein folds. The nsP2pro C-terminal domain displays structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and provides essential elements that contribute to substrate recognition and may also regulate the structure of the substrate binding cleft.

==About this Structure==

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[[Category: Single protein]]

[[Category: Venezuelan equine encephalitis virus]]

[[Category: Russo, A.T.]]

[[Category: Russo, A T.]]

[[Category: Watowich, S.J.]]

[[Category: Watowich, S J.]]

[[Category: White, M.A.]]

[[Category: White, M A.]]

[[Category: FMT]]

[[Category: alpha/beta/alpha]]

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[[Category: rossman fold]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Alphavirus replication and propagation is dependent on the protease, activity of the viral nsP2 protein, which cleaves the nsP1234 polyprotein, replication complex into functional components. Thus, nsP2 is an, attractive target for drug discovery efforts to combat highly pathogenic, alphaviruses. Unfortunately, antiviral development has been hampered by a, lack of structural information for the nsP2 protease. Here, we report the, crystal structure of the nsP2 protease (nsP2pro) from Venezuelan equine, encephalitis alphavirus determined at 2.45 A resolution. The protease, structure consists of two distinct domains. The nsP2pro N-terminal domain, contains the catalytic dyad cysteine and histidine residues organized in a, protein fold that differs significantly from any known cysteine protease, or protein folds. The nsP2pro C-terminal domain displays structural, similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and, provides essential elements that contribute to substrate recognition and, may also regulate the structure of the substrate binding cleft.
+Alphavirus replication and propagation is dependent on the protease activity of the viral nsP2 protein, which cleaves the nsP1234 polyprotein replication complex into functional components. Thus, nsP2 is an attractive target for drug discovery efforts to combat highly pathogenic alphaviruses. Unfortunately, antiviral development has been hampered by a lack of structural information for the nsP2 protease. Here, we report the crystal structure of the nsP2 protease (nsP2pro) from Venezuelan equine encephalitis alphavirus determined at 2.45 A resolution. The protease structure consists of two distinct domains. The nsP2pro N-terminal domain contains the catalytic dyad cysteine and histidine residues organized in a protein fold that differs significantly from any known cysteine protease or protein folds. The nsP2pro C-terminal domain displays structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and provides essential elements that contribute to substrate recognition and may also regulate the structure of the substrate binding cleft.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Venezuelan equine encephalitis virus]]
-[[Category: Russo, A.T.]]
+[[Category: Russo, A T.]]
-[[Category: Watowich, S.J.]]
+[[Category: Watowich, S J.]]
-[[Category: White, M.A.]]
+[[Category: White, M A.]]
 [[Category: FMT]]
 [[Category: alpha/beta/alpha]]
@@ Line 21: / Line 21: @@
 [[Category: rossman fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:30:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:31 2008''