1zci
From Proteopedia
(New page: 200px<br /> <applet load="1zci" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zci, resolution 1.65Å" /> '''HIV-1 DIS RNA subty...) |
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| - | [[Image:1zci.gif|left|200px]]<br /> | + | [[Image:1zci.gif|left|200px]]<br /><applet load="1zci" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zci" size=" | + | |
caption="1zci, resolution 1.65Å" /> | caption="1zci, resolution 1.65Å" /> | ||
'''HIV-1 DIS RNA subtype F- monoclinic form'''<br /> | '''HIV-1 DIS RNA subtype F- monoclinic form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | All retroviruses encapsidate their genome as a dimer of homologous | + | All retroviruses encapsidate their genome as a dimer of homologous single-stranded RNAs. The dimerization initiation site (DIS) of human immunodeficiency virus type 1 (HIV-1) is located in the 5'-untranslated region of the viral genome and consists of a hairpin with a 6 nt self-complementary loop sequence. Genomic RNA dimerization, a crucial step for virion infectivity, is promoted by the formation of a loop-loop complex (or kissing complex) between two DIS hairpins. Crystal structures for the subtypes A, B and F of the HIV-1 DIS kissing complex have now been solved at 2.3 A, 1.9 A and 1.6 A, respectively. They revealed a polymorphism of bulged-out residues showing clearly that their conformation is not a mere consequence of crystal packing. They also provide more insights into ion binding, hydration, and RNA conformation and flexibility. In particular, we observed the binding of spermine to the loop-loop helix, which displaced a magnesium cation important for subtype A DIS dimerization. The excellent agreement between X-ray structures and the results of chemical probing and interference data on larger viral RNA fragments shows that the crystal structures are relevant for the DIS kissing complex present in solution and in viral particles. Accordingly, these structures will be helpful for designing new drugs derived from aminoglycoside antibiotics and targeted against the RNA dimerization step of the viral life-cycle. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZCI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZCI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rna]] | [[Category: rna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:11 2008'' |
Revision as of 14:14, 21 February 2008
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HIV-1 DIS RNA subtype F- monoclinic form
Overview
All retroviruses encapsidate their genome as a dimer of homologous single-stranded RNAs. The dimerization initiation site (DIS) of human immunodeficiency virus type 1 (HIV-1) is located in the 5'-untranslated region of the viral genome and consists of a hairpin with a 6 nt self-complementary loop sequence. Genomic RNA dimerization, a crucial step for virion infectivity, is promoted by the formation of a loop-loop complex (or kissing complex) between two DIS hairpins. Crystal structures for the subtypes A, B and F of the HIV-1 DIS kissing complex have now been solved at 2.3 A, 1.9 A and 1.6 A, respectively. They revealed a polymorphism of bulged-out residues showing clearly that their conformation is not a mere consequence of crystal packing. They also provide more insights into ion binding, hydration, and RNA conformation and flexibility. In particular, we observed the binding of spermine to the loop-loop helix, which displaced a magnesium cation important for subtype A DIS dimerization. The excellent agreement between X-ray structures and the results of chemical probing and interference data on larger viral RNA fragments shows that the crystal structures are relevant for the DIS kissing complex present in solution and in viral particles. Accordingly, these structures will be helpful for designing new drugs derived from aminoglycoside antibiotics and targeted against the RNA dimerization step of the viral life-cycle.
About this Structure
1ZCI is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Polymorphism of bulged-out residues in HIV-1 RNA DIS kissing complex and structure comparison with solution studies., Ennifar E, Dumas P, J Mol Biol. 2006 Feb 24;356(3):771-82. Epub 2005 Dec 21. PMID:16403527
Page seeded by OCA on Thu Feb 21 16:14:11 2008
Categories: Protein complex | Dumas, P. | Ennifar, E. | K | Hiv-1 | Loop-loop complex | Metal ions | Rna
