1duq

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(New page: 200px<br /> <applet load="1duq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1duq, resolution 2.10&Aring;" /> '''CRYSTAL STRUCTURE O...)
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<applet load="1duq" size="450" color="white" frame="true" align="right" spinBox="true"
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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==
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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.
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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==
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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].
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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]]
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[[Category: Holbrook, E.L.]]
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[[Category: Holbrook, E L.]]
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[[Category: Holbrook, S.R.]]
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[[Category: Holbrook, S R.]]
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[[Category: Hung, L.W.]]
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[[Category: Hung, L W.]]
[[Category: NA]]
[[Category: NA]]
[[Category: hiv-1]]
[[Category: hiv-1]]
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[[Category: rre]]
[[Category: rre]]
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Revision as of 10:20, 21 February 2008


1duq, resolution 2.10Å

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CRYSTAL STRUCTURE OF THE REV BINDING ELEMENT OF HIV-1

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.

About this Structure

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

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:10792052

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