2buo: Difference between revisions

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[[Image:2buo.~~gif~~|left|200px]]

[[Image:2buo.png|left|200px]]

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~~'''~~HIV-1 CAPSID C-TERMINAL DOMAIN IN COMPLEX WITH AN INHIBITOR OF PARTICLE ASSEMBLY~~'''~~

===HIV-1 CAPSID C-TERMINAL DOMAIN IN COMPLEX WITH AN INHIBITOR OF PARTICLE ASSEMBLY===

~~==Overview==~~

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~~Immature HIV particles bud from infected cells after assembly at the cytoplasmic side of cellular membranes. This assembly is driven by interactions between Gag polyproteins. Mature particles~~, ~~each containing a characteristic conical core~~, ~~are later generated by proteolytic maturation of Gag in~~ the ~~virion. The C-terminal domain of~~ the ~~HIV-1 capsid protein~~ (~~C-CA~~) ~~has been shown to contain oligomerization determinants essential for particle assembly. Here we report~~ the 1.7-A-resolution crystal structure of C-CA in complex with a peptide capable of inhibiting immature- and mature-like particle assembly in vitro. The peptide inserts as an amphipathic alpha-helix into a conserved hydrophobic groove of C-CA, resulting in formation of a compact five-helix bundle with altered dimeric interactions. This structure thus reveals the details of an allosteric site in the HIV capsid protein that can be targeted for antiviral therapy.

The line below this paragraph, {{ABSTRACT_PUBMED_16041386}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16041386 is the PubMed ID number.

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==About this Structure==

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[[Category: Inhibitor]]

[[Category: Polyprotein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 20~~:49:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:07:55 2008''

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-[[Image:2buo.gif|left|200px]]
+{{Seed}}
+[[Image:2buo.png|left|200px]]
 <!--
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 {{STRUCTURE_2buo|  PDB=2buo  |  SCENE=  }}
-'''HIV-1 CAPSID C-TERMINAL DOMAIN IN COMPLEX WITH AN INHIBITOR OF PARTICLE ASSEMBLY'''
+===HIV-1 CAPSID C-TERMINAL DOMAIN IN COMPLEX WITH AN INHIBITOR OF PARTICLE ASSEMBLY===
-==Overview==
+<!--
-Immature HIV particles bud from infected cells after assembly at the cytoplasmic side of cellular membranes. This assembly is driven by interactions between Gag polyproteins. Mature particles, each containing a characteristic conical core, are later generated by proteolytic maturation of Gag in the virion. The C-terminal domain of the HIV-1 capsid protein (C-CA) has been shown to contain oligomerization determinants essential for particle assembly. Here we report the 1.7-A-resolution crystal structure of C-CA in complex with a peptide capable of inhibiting immature- and mature-like particle assembly in vitro. The peptide inserts as an amphipathic alpha-helix into a conserved hydrophobic groove of C-CA, resulting in formation of a compact five-helix bundle with altered dimeric interactions. This structure thus reveals the details of an allosteric site in the HIV capsid protein that can be targeted for antiviral therapy.
+The line below this paragraph, {{ABSTRACT_PUBMED_16041386}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16041386 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16041386}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Inhibitor]]
 [[Category: Polyprotein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:49:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:07:55 2008''