2bx3: Difference between revisions

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[[Image:2bx3.gif|left|200px]]<br /><applet load="2bx3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bx3.gif|left|200px]]<br /><applet load="2bx3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bx3, resolution 2.00Å" />

'''CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P43212)'''<br />

==Overview==

The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the, processing of the viral polyproteins and thus an attractive target for the, discovery of drugs directed against SARS. The enzyme has been shown by, X-ray crystallography to undergo significant pH-dependent conformational, changes. Here, we assess the conformational flexibility of the M(pro) by, analysis of multiple crystal structures (including two new crystal forms), and by molecular dynamics (MD) calculations. The MD simulations take into, account the different protonation states of two histidine residues in the, substrate-binding site and explain the pH-activity profile of the enzyme., The low enzymatic activity of the M(pro) monomer and the need for, dimerization are also discussed.

The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the processing of the viral polyproteins and thus an attractive target for the discovery of drugs directed against SARS. The enzyme has been shown by X-ray crystallography to undergo significant pH-dependent conformational changes. Here, we assess the conformational flexibility of the M(pro) by analysis of multiple crystal structures (including two new crystal forms) and by molecular dynamics (MD) calculations. The MD simulations take into account the different protonation states of two histidine residues in the substrate-binding site and explain the pH-activity profile of the enzyme. The low enzymatic activity of the M(pro) monomer and the need for dimerization are also discussed.

==About this Structure==

2BX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BX3 OCA].

2BX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX3 OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Hilgenfeld, R.]]

[[Category: Mesters, J.R.]]

[[Category: Mesters, J R.]]

[[Category: Verschueren, K.H.G.]]

[[Category: Verschueren, K H.G.]]

[[Category: anti-parallel a-helices]]

[[Category: anti-parallel b-barrel]]

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[[Category: viral protein]]

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@@ Line 1: / Line 1: @@
-[[Image:2bx3.gif|left|200px]]<br /><applet load="2bx3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bx3.gif|left|200px]]<br /><applet load="2bx3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bx3, resolution 2.00&Aring;" />
 '''CRYSTAL STRUCTURE OF SARS CORONAVIRUS MAIN PROTEINASE (P43212)'''<br />
 ==Overview==
-The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the, processing of the viral polyproteins and thus an attractive target for the, discovery of drugs directed against SARS. The enzyme has been shown by, X-ray crystallography to undergo significant pH-dependent conformational, changes. Here, we assess the conformational flexibility of the M(pro) by, analysis of multiple crystal structures (including two new crystal forms), and by molecular dynamics (MD) calculations. The MD simulations take into, account the different protonation states of two histidine residues in the, substrate-binding site and explain the pH-activity profile of the enzyme., The low enzymatic activity of the M(pro) monomer and the need for, dimerization are also discussed.
+The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the processing of the viral polyproteins and thus an attractive target for the discovery of drugs directed against SARS. The enzyme has been shown by X-ray crystallography to undergo significant pH-dependent conformational changes. Here, we assess the conformational flexibility of the M(pro) by analysis of multiple crystal structures (including two new crystal forms) and by molecular dynamics (MD) calculations. The MD simulations take into account the different protonation states of two histidine residues in the substrate-binding site and explain the pH-activity profile of the enzyme. The low enzymatic activity of the M(pro) monomer and the need for dimerization are also discussed.
 ==About this Structure==
-BX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BX3 OCA].
+BX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX3 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Hilgenfeld, R.]]
-[[Category: Mesters, J.R.]]
+[[Category: Mesters, J R.]]
-[[Category: Verschueren, K.H.G.]]
+[[Category: Verschueren, K H.G.]]
 [[Category: anti-parallel a-helices]]
 [[Category: anti-parallel b-barrel]]
@@ Line 22: / Line 22: @@
 [[Category: viral protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:56:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:30 2008''