1a5w: Difference between revisions

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==Overview==

The x-ray structures of an inhibitor complex of the catalytic core domain, of avian sarcoma virus integrase (ASV IN) were solved at 1.9- to 2.0-A, resolution at two pH values, with and without Mn2+ cations. This inhibitor, (Y-3), originally identified in a screen for inhibitors of the catalytic, activity of HIV type 1 integrase (HIV-1 IN), was found in the present, study to be active against ASV IN as well as HIV-1 IN. The Y-3 molecule is, located in close proximity to the enzyme active site, interacts with the, flexible loop, alters loop conformation, and affects the conformations of, active site residues. As crystallized, a Y-3 molecule stacks against its, symmetry-related mate. Preincubation of IN with metal cations does not, prevent inhibition, and Y-3 binding does not prevent binding of divalent, cations to IN. Three compounds chemically related to Y-3 also were, investigated, but no binding was observed in the crystals. Our results, identify the structural elements of the inhibitor that likely determine, its binding properties.

The x-ray structures of an inhibitor complex of the catalytic core domain of avian sarcoma virus integrase (ASV IN) were solved at 1.9- to 2.0-A resolution at two pH values, with and without Mn2+ cations. This inhibitor (Y-3), originally identified in a screen for inhibitors of the catalytic activity of HIV type 1 integrase (HIV-1 IN), was found in the present study to be active against ASV IN as well as HIV-1 IN. The Y-3 molecule is located in close proximity to the enzyme active site, interacts with the flexible loop, alters loop conformation, and affects the conformations of active site residues. As crystallized, a Y-3 molecule stacks against its symmetry-related mate. Preincubation of IN with metal cations does not prevent inhibition, and Y-3 binding does not prevent binding of divalent cations to IN. Three compounds chemically related to Y-3 also were investigated, but no binding was observed in the crystals. Our results identify the structural elements of the inhibitor that likely determine its binding properties.

==About this Structure==

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[[Category: hydrolase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The x-ray structures of an inhibitor complex of the catalytic core domain, of avian sarcoma virus integrase (ASV IN) were solved at 1.9- to 2.0-A, resolution at two pH values, with and without Mn2+ cations. This inhibitor, (Y-3), originally identified in a screen for inhibitors of the catalytic, activity of HIV type 1 integrase (HIV-1 IN), was found in the present, study to be active against ASV IN as well as HIV-1 IN. The Y-3 molecule is, located in close proximity to the enzyme active site, interacts with the, flexible loop, alters loop conformation, and affects the conformations of, active site residues. As crystallized, a Y-3 molecule stacks against its, symmetry-related mate. Preincubation of IN with metal cations does not, prevent inhibition, and Y-3 binding does not prevent binding of divalent, cations to IN. Three compounds chemically related to Y-3 also were, investigated, but no binding was observed in the crystals. Our results, identify the structural elements of the inhibitor that likely determine, its binding properties.
+The x-ray structures of an inhibitor complex of the catalytic core domain of avian sarcoma virus integrase (ASV IN) were solved at 1.9- to 2.0-A resolution at two pH values, with and without Mn2+ cations. This inhibitor (Y-3), originally identified in a screen for inhibitors of the catalytic activity of HIV type 1 integrase (HIV-1 IN), was found in the present study to be active against ASV IN as well as HIV-1 IN. The Y-3 molecule is located in close proximity to the enzyme active site, interacts with the flexible loop, alters loop conformation, and affects the conformations of active site residues. As crystallized, a Y-3 molecule stacks against its symmetry-related mate. Preincubation of IN with metal cations does not prevent inhibition, and Y-3 binding does not prevent binding of divalent cations to IN. Three compounds chemically related to Y-3 also were investigated, but no binding was observed in the crystals. Our results identify the structural elements of the inhibitor that likely determine its binding properties.
 ==About this Structure==
@@ Line 23: / Line 23: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:29:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:11 2008''