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Title: The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution. Author: Ippolito JA, Steitz TA. Journal: J Mol Biol; 2000 Jan 28; 295(4):711-7. PubMed ID: 10656783. 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.[Abstract] [Full Text] [Related] [New Search]