Sandbox Reserved 1502: Difference between revisions
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'''The three domain of the HIV integrase:''' | '''The three domain of the HIV integrase:''' | ||
[[Image:Domain_HIV_Integrase.jpg]] | [[Image:Domain_HIV_Integrase.jpg]] [http://www.jbc.org/content/276/26/23213.full] | ||
'''HIV Integrase sequence:''' | '''HIV Integrase sequence:''' | ||
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The catalytic core domain contains three acidic residues, the D,D-35-E motif, comprising residues Asp64, Asp116, and Glu152. By analogy with models of catalysis by DNA polymerases, it has been proposed that coordination of divalent metal ion to these residues plays a key role in catalysis. The catalytic residues Asp64, Asp116, and Glu152of HIV-1 integrase and their counterparts in the ASV structures are in close proximity, coordinate divalent metal ion, and define the active site. However, the residues comprising the active site region exhibit considerable flexibility, suggesting that binding of DNA substrate is required to impose the precise configuration of residues that are required for catalysis. | The catalytic core domain contains three acidic residues, the D,D-35-E motif, comprising residues Asp64, Asp116, and Glu152. By analogy with models of catalysis by DNA polymerases, it has been proposed that coordination of divalent metal ion to these residues plays a key role in catalysis. The catalytic residues Asp64, Asp116, and Glu152of HIV-1 integrase and their counterparts in the ASV structures are in close proximity, coordinate divalent metal ion, and define the active site. However, the residues comprising the active site region exhibit considerable flexibility, suggesting that binding of DNA substrate is required to impose the precise configuration of residues that are required for catalysis. | ||
[[Image:Core enzyme.jpg]] | [[Image:Core enzyme.jpg]] [http://www.jbc.org/content/276/26/23213.full] | ||
<scene name='80/802676/Core_enzyme/2'>Here is the 3D structure of the core domain</scene> | <scene name='80/802676/Core_enzyme/2'>Here is the 3D structure of the core domain</scene> | ||
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====Structure and role of the N ter domain==== | ====Structure and role of the N ter domain==== | ||
The N-terminal domain of HIV-1 integrase contains a conserved pair of His and Cys residues, a motif similar to the zinc-coordinating residues of zinc fingers. This domain binds zinc but its structure is totally different from that of zinc fingers. It consists of a bundle of three α-helices. | The N-terminal domain of HIV-1 integrase contains a conserved pair of His and Cys residues, a motif similar to the zinc-coordinating residues of zinc fingers. This domain binds zinc but its structure is totally different from that of zinc fingers. It consists of a bundle of three α-helices. This domain is necessary for the oligomerization of the integrase. | ||
[[Image:Nter-domain.jpg]] | [[Image:Nter-domain.jpg]] [http://www.jbc.org/content/276/26/23213.full] | ||
<scene name='80/802676/N-ter_domain/2'>Here is the 3D structure of the N-ter domain of the HIV integrase</scene> | <scene name='80/802676/N-ter_domain/2'>Here is the 3D structure of the N-ter domain of the HIV integrase</scene> | ||
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====Structure and role of the C ter domain==== | ====Structure and role of the C ter domain==== | ||
[[Image:C-ter domain.jpg]] | Here is the structure of the C-ter domain : | ||
[[Image:C-ter domain.jpg]] [http://www.jbc.org/content/276/26/23213.full] | |||
The C-ter domain has a non-specific DNA binding activity. | |||