1duq
From Proteopedia
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|PDB= 1duq |SIZE=350|CAPTION= <scene name='initialview01'>1duq</scene>, resolution 2.10Å | |PDB= 1duq |SIZE=350|CAPTION= <scene name='initialview01'>1duq</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1duq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1duq OCA], [http://www.ebi.ac.uk/pdbsum/1duq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1duq RCSB]</span> | ||
}} | }} | ||
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[[Category: Holbrook, S R.]] | [[Category: Holbrook, S R.]] | ||
[[Category: Hung, L W.]] | [[Category: Hung, L W.]] | ||
| - | [[Category: NA]] | ||
[[Category: hiv-1]] | [[Category: hiv-1]] | ||
[[Category: rev binding domain]] | [[Category: rev binding domain]] | ||
[[Category: rre]] | [[Category: rre]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:03 2008'' |
Revision as of 16:49, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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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