The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution.
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.
Ippolito
J A
JA
Department of Molecular Biophysics, Howard Hughes Medical Institute, New Haven, CT 06520-8114, USA.
Steitz
T A
TA
D001483:Base Sequence; D018360:Crystallography, X-Ray / Q000379:methods; D015497:HIV-1 / Q000235:genetics*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D012367:RNA, Viral / Q000737:chemistry*
D012367:RNA, Viral