1duq: Difference between revisions

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New page: left|200px<br /> <applet load="1duq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1duq, resolution 2.10Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1duq.gif|left|200px]]<br />
[[Image:1duq.gif|left|200px]]<br /><applet load="1duq" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1duq" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1duq, resolution 2.10&Aring;" />
caption="1duq, resolution 2.10&Aring;" />
'''CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1'''<br />
'''CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1'''<br />


==Overview==
==Overview==
The crystal and molecular structure of an RNA duplex corresponding to the, high affinity Rev protein binding element (RBE) has been determined at, 2.1-A resolution. Four unique duplexes are present in the crystal, comprising two structural variants. In each duplex, the RNA double helix, consists of an annealed 12-mer and 14-mer that form an asymmetric internal, loop consisting of G-G and G-A noncanonical base pairs and a flipped-out, uridine. The 12-mer strand has an A-form conformation, whereas the 14-mer, strand is distorted to accommodate the bulges and noncanonical base, pairing. In contrast to the NMR model of the unbound RBE, an asymmetric, G-G pair with N2-N7 and N1-O6 hydrogen bonding, is formed in each helix., The G-A base pairing agrees with the NMR structure in one structural, variant, but forms a novel water-mediated pair in the other. A backbone, flip and reorientation of the G-G base pair is required to assume the RBE, conformation present in the NMR model of the complex between the RBE and, the Rev peptide.
The crystal and molecular structure of an RNA duplex corresponding to the high affinity Rev protein binding element (RBE) has been determined at 2.1-A resolution. Four unique duplexes are present in the crystal, comprising two structural variants. In each duplex, the RNA double helix consists of an annealed 12-mer and 14-mer that form an asymmetric internal loop consisting of G-G and G-A noncanonical base pairs and a flipped-out uridine. The 12-mer strand has an A-form conformation, whereas the 14-mer strand is distorted to accommodate the bulges and noncanonical base pairing. In contrast to the NMR model of the unbound RBE, an asymmetric G-G pair with N2-N7 and N1-O6 hydrogen bonding, is formed in each helix. The G-A base pairing agrees with the NMR structure in one structural variant, but forms a novel water-mediated pair in the other. A backbone flip and reorientation of the G-G base pair is required to assume the RBE conformation present in the NMR model of the complex between the RBE and the Rev peptide.


==About this Structure==
==About this Structure==
1DUQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DUQ OCA].  
1DUQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUQ OCA].  


==Reference==
==Reference==
The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variability., Hung LW, Holbrook EL, Holbrook SR, Proc Natl Acad Sci U S A. 2000 May 9;97(10):5107-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10792052 10792052]
The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variability., Hung LW, Holbrook EL, Holbrook SR, Proc Natl Acad Sci U S A. 2000 May 9;97(10):5107-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10792052 10792052]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Holbrook, E.L.]]
[[Category: Holbrook, E L.]]
[[Category: Holbrook, S.R.]]
[[Category: Holbrook, S R.]]
[[Category: Hung, L.W.]]
[[Category: Hung, L W.]]
[[Category: NA]]
[[Category: NA]]
[[Category: hiv-1]]
[[Category: hiv-1]]
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[[Category: rre]]
[[Category: rre]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:59:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:43 2008''

Revision as of 13:20, 21 February 2008

File:1duq.gif


1duq, resolution 2.10Å

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CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1

OverviewOverview

The crystal and molecular structure of an RNA duplex corresponding to the high affinity Rev protein binding element (RBE) has been determined at 2.1-A resolution. Four unique duplexes are present in the crystal, comprising two structural variants. In each duplex, the RNA double helix consists of an annealed 12-mer and 14-mer that form an asymmetric internal loop consisting of G-G and G-A noncanonical base pairs and a flipped-out uridine. The 12-mer strand has an A-form conformation, whereas the 14-mer strand is distorted to accommodate the bulges and noncanonical base pairing. In contrast to the NMR model of the unbound RBE, an asymmetric G-G pair with N2-N7 and N1-O6 hydrogen bonding, is formed in each helix. The G-A base pairing agrees with the NMR structure in one structural variant, but forms a novel water-mediated pair in the other. A backbone flip and reorientation of the G-G base pair is required to assume the RBE conformation present in the NMR model of the complex between the RBE and the Rev peptide.

About this StructureAbout this Structure

1DUQ is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the Rev binding element of HIV-1 reveals novel base pairing and conformational variability., Hung LW, Holbrook EL, Holbrook SR, Proc Natl Acad Sci U S A. 2000 May 9;97(10):5107-12. PMID:10792052

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