1ex4: Difference between revisions

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[[Image:1ex4.gif|left|200px]]<br />

[[Image:1ex4.gif|left|200px]]<br /><applet load="1ex4" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1ex4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ex4, resolution 2.80Å" />

'''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN'''<br />

==Overview==

Insolubility of full-length HIV-1 integrase (IN) limited previous, structure analyses to individual domains. By introducing five point, mutations, we engineered a more soluble IN that allowed us to generate, multidomain HIV-1 IN crystals. The first multidomain HIV-1 IN structure is, reported. It incorporates the catalytic core and C-terminal domains, (residues 52-288). The structure resolved to 2.8 A is a Y-shaped dimer., Within the dimer, the catalytic core domains form the only dimer, interface, and the C-terminal domains are located 55 A apart. A 26-aa, alpha-helix, alpha6, links the C-terminal domain to the catalytic core. A, kink in one of the two alpha6 helices occurs near a known proteolytic, site, suggesting that it may act as a flexible elbow to reorient the, domains during the integration process. Two proteins that bind DNA in a, sequence-independent manner are structurally homologous to the HIV-1 IN, C-terminal domain, suggesting a similar protein-DNA interaction in which, the IN C-terminal domain may serve to bind, bend, and orient viral DNA, during integration. A strip of positively charged amino acids contributed, by both monomers emerges from each active site of the dimer, suggesting a, minimally dimeric platform for binding each viral DNA end. The crystal, structure of the isolated catalytic core domain (residues 52-210), independently determined at 1.6-A resolution, is identical to the core, domain within the two-domain 52-288 structure.

Insolubility of full-length HIV-1 integrase (IN) limited previous structure analyses to individual domains. By introducing five point mutations, we engineered a more soluble IN that allowed us to generate multidomain HIV-1 IN crystals. The first multidomain HIV-1 IN structure is reported. It incorporates the catalytic core and C-terminal domains (residues 52-288). The structure resolved to 2.8 A is a Y-shaped dimer. Within the dimer, the catalytic core domains form the only dimer interface, and the C-terminal domains are located 55 A apart. A 26-aa alpha-helix, alpha6, links the C-terminal domain to the catalytic core. A kink in one of the two alpha6 helices occurs near a known proteolytic site, suggesting that it may act as a flexible elbow to reorient the domains during the integration process. Two proteins that bind DNA in a sequence-independent manner are structurally homologous to the HIV-1 IN C-terminal domain, suggesting a similar protein-DNA interaction in which the IN C-terminal domain may serve to bind, bend, and orient viral DNA during integration. A strip of positively charged amino acids contributed by both monomers emerges from each active site of the dimer, suggesting a minimally dimeric platform for binding each viral DNA end. The crystal structure of the isolated catalytic core domain (residues 52-210), independently determined at 1.6-A resolution, is identical to the core domain within the two-domain 52-288 structure.

==About this Structure==

1EX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with CPS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1EX4 OCA].

1EX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=CPS:'>CPS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EX4 OCA].

==Reference==

Line 14:

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[[Category: Human immunodeficiency virus 1]]

[[Category: Single protein]]

[[Category: Chen, J.C.H.]]

[[Category: Chen, J C.H.]]

[[Category: Finer-Moore, J.S.]]

[[Category: Finer-Moore, J S.]]

[[Category: Krucinski, J.]]

[[Category: Leavitt, A.D.]]

[[Category: Leavitt, A D.]]

[[Category: Miercke, L.J.W.]]

[[Category: Miercke, L J.W.]]

[[Category: Stroud, R.M.]]

[[Category: Stroud, R M.]]

[[Category: Tang, A.H.]]

[[Category: Tang, A H.]]

[[Category: CPS]]

[[Category: cis-proline]]

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[[Category: sh3-like domain]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:24 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ex4.gif|left|200px]]<br />
+[[Image:1ex4.gif|left|200px]]<br /><applet load="1ex4" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ex4" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ex4, resolution 2.80&Aring;" />
 '''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN'''<br />
 ==Overview==
-Insolubility of full-length HIV-1 integrase (IN) limited previous, structure analyses to individual domains. By introducing five point, mutations, we engineered a more soluble IN that allowed us to generate, multidomain HIV-1 IN crystals. The first multidomain HIV-1 IN structure is, reported. It incorporates the catalytic core and C-terminal domains, (residues 52-288). The structure resolved to 2.8 A is a Y-shaped dimer., Within the dimer, the catalytic core domains form the only dimer, interface, and the C-terminal domains are located 55 A apart. A 26-aa, alpha-helix, alpha6, links the C-terminal domain to the catalytic core. A, kink in one of the two alpha6 helices occurs near a known proteolytic, site, suggesting that it may act as a flexible elbow to reorient the, domains during the integration process. Two proteins that bind DNA in a, sequence-independent manner are structurally homologous to the HIV-1 IN, C-terminal domain, suggesting a similar protein-DNA interaction in which, the IN C-terminal domain may serve to bind, bend, and orient viral DNA, during integration. A strip of positively charged amino acids contributed, by both monomers emerges from each active site of the dimer, suggesting a, minimally dimeric platform for binding each viral DNA end. The crystal, structure of the isolated catalytic core domain (residues 52-210), independently determined at 1.6-A resolution, is identical to the core, domain within the two-domain 52-288 structure.
+Insolubility of full-length HIV-1 integrase (IN) limited previous structure analyses to individual domains. By introducing five point mutations, we engineered a more soluble IN that allowed us to generate multidomain HIV-1 IN crystals. The first multidomain HIV-1 IN structure is reported. It incorporates the catalytic core and C-terminal domains (residues 52-288). The structure resolved to 2.8 A is a Y-shaped dimer. Within the dimer, the catalytic core domains form the only dimer interface, and the C-terminal domains are located 55 A apart. A 26-aa alpha-helix, alpha6, links the C-terminal domain to the catalytic core. A kink in one of the two alpha6 helices occurs near a known proteolytic site, suggesting that it may act as a flexible elbow to reorient the domains during the integration process. Two proteins that bind DNA in a sequence-independent manner are structurally homologous to the HIV-1 IN C-terminal domain, suggesting a similar protein-DNA interaction in which the IN C-terminal domain may serve to bind, bend, and orient viral DNA during integration. A strip of positively charged amino acids contributed by both monomers emerges from each active site of the dimer, suggesting a minimally dimeric platform for binding each viral DNA end. The crystal structure of the isolated catalytic core domain (residues 52-210), independently determined at 1.6-A resolution, is identical to the core domain within the two-domain 52-288 structure.
 ==About this Structure==
-EX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with CPS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EX4 OCA].
+EX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=CPS:'>CPS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EX4 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Human immunodeficiency virus 1]]
 [[Category: Single protein]]
-[[Category: Chen, J.C.H.]]
+[[Category: Chen, J C.H.]]
-[[Category: Finer-Moore, J.S.]]
+[[Category: Finer-Moore, J S.]]
 [[Category: Krucinski, J.]]
-[[Category: Leavitt, A.D.]]
+[[Category: Leavitt, A D.]]
-[[Category: Miercke, L.J.W.]]
+[[Category: Miercke, L J.W.]]
-[[Category: Stroud, R.M.]]
+[[Category: Stroud, R M.]]
-[[Category: Tang, A.H.]]
+[[Category: Tang, A H.]]
 [[Category: CPS]]
 [[Category: cis-proline]]
@@ Line 26: / Line 25: @@
 [[Category: sh3-like domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 14:01:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:24 2008''