1CSL

CRYSTAL STRUCTURE OF THE RRE HIGH AFFINITY SITE

Summary for 1CSL

• Entry DOI: 10.2210/pdb1csl/pdb
• Descriptor: 5'-R(*AP*AP*CP*GP*GP*GP*CP*GP*CP*AP*GP*AP*A)-3', 5'-R(*UP*CP*UP*GP*AP*CP*GP*GP*UP*AP*CP*GP*UP*UP*U)-3' (3 entities in total)
• Functional Keywords: rre high affinity site, hiv-1, rna
• Total number of polymer chains: 2
• Total formula weight: 8989.46

Authors

Ippolito, J.A.,Steitz, T.A. (deposition date: 1999-08-18, release date: 2000-02-14, Last modification date: 2024-02-07)

Primary citation

Ippolito, J.A.,Steitz, T.A.
The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution.
J.Mol.Biol., 295:711-717, 2000

PubMed Abstract: The crystal structure of a 28 nt RNA fragment containing the human immunodeficiency virus type 1 (HIV-1) Rev response element high affinity binding site for Rev protein has been solved at 1.6 A resolution. The overall structure of the RRE helix is greatly distorted from A-form geometry by the presence of two purine-purine base-pairs and two single nucleotide bulges. G48 and G71 form a Hoogsteen-type asymmetric base-pair with G71 adopting a syn conformation. The non-canonical regions in the unliganded Rev response element molecule narrow the major groove width with respect to standard A-RNA. The Rev response element structure observed here represents a closed form of the Rev binding site and differs from conformations of the RNA observed previously by solution NMR studies.

PubMed: 10656783
DOI: 10.1006/jmbi.1999.3405

Experimental method

X-RAY DIFFRACTION (1.6 Å)