2p4d: Difference between revisions

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==Overview==

Variola major virus, the causative agent of smallpox, encodes the, dual-specificity H1 phosphatase. Because this enzyme is essential for the, production of mature virus particles, it is an attractive molecular target, for the development of therapeutic countermeasures for this potential, agent of bioterrorism. As a first step in this direction, the crystal, structure of H1 phosphatase has been determined at a resolution of 1.8 A., In silico screening methods have led to the identification of several, small molecules that inhibit Variola H1 phosphatase with IC(50) values in, the low micromolar range. These molecules provide novel leads for future, drug development.

Variola major virus, the causative agent of smallpox, encodes the dual-specificity H1 phosphatase. Because this enzyme is essential for the production of mature virus particles, it is an attractive molecular target for the development of therapeutic countermeasures for this potential agent of bioterrorism. As a first step in this direction, the crystal structure of H1 phosphatase has been determined at a resolution of 1.8 A. In silico screening methods have led to the identification of several small molecules that inhibit Variola H1 phosphatase with IC(50) values in the low micromolar range. These molecules provide novel leads for future drug development.

==About this Structure==

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[[Category: Variola virus]]

[[Category: Phan, J.]]

[[Category: Tropea, J.E.]]

[[Category: Tropea, J E.]]

[[Category: Waugh, D.S.]]

[[Category: Waugh, D S.]]

[[Category: drug design]]

[[Category: dual specificity phosphatase]]

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[[Category: small pox]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Variola major virus, the causative agent of smallpox, encodes the, dual-specificity H1 phosphatase. Because this enzyme is essential for the, production of mature virus particles, it is an attractive molecular target, for the development of therapeutic countermeasures for this potential, agent of bioterrorism. As a first step in this direction, the crystal, structure of H1 phosphatase has been determined at a resolution of 1.8 A., In silico screening methods have led to the identification of several, small molecules that inhibit Variola H1 phosphatase with IC(50) values in, the low micromolar range. These molecules provide novel leads for future, drug development.
+Variola major virus, the causative agent of smallpox, encodes the dual-specificity H1 phosphatase. Because this enzyme is essential for the production of mature virus particles, it is an attractive molecular target for the development of therapeutic countermeasures for this potential agent of bioterrorism. As a first step in this direction, the crystal structure of H1 phosphatase has been determined at a resolution of 1.8 A. In silico screening methods have led to the identification of several small molecules that inhibit Variola H1 phosphatase with IC(50) values in the low micromolar range. These molecules provide novel leads for future drug development.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Variola virus]]
 [[Category: Phan, J.]]
-[[Category: Tropea, J.E.]]
+[[Category: Tropea, J E.]]
-[[Category: Waugh, D.S.]]
+[[Category: Waugh, D S.]]
 [[Category: drug design]]
 [[Category: dual specificity phosphatase]]
@@ Line 21: / Line 21: @@
 [[Category: small pox]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:07:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:41 2008''