Structural highlights
Publication Abstract from PubMed
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.
The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution.,Ippolito JA, Steitz TA J Mol Biol. 2000 Jan 28;295(4):711-7. PMID:10656783[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ippolito JA, Steitz TA. The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution. J Mol Biol. 2000 Jan 28;295(4):711-7. PMID:10656783 doi:10.1006/jmbi.1999.3405
