3LPH

Crystal structure of the HIV-1 Rev dimer

3LPH の概要

• エントリーDOI: 10.2210/pdb3lph/pdb
• 分子名称: Protein Rev, SULFATE ION, BROMIDE ION, ... (5 entities in total)
• 機能のキーワード: helix-loop-helix, rna-binding arginine rich motif, protein oligomerization, aids, host cytoplasm, host nucleus, host-virus interaction, mrna transport, phosphoprotein, rna-binding, transport, viral protein
• 由来する生物種: Human immunodeficiency virus type 1 (HIV-1)
• 細胞内の位置: Host nucleus, host nucleolus : P69718
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 35188.79

構造登録者

Daugherty, M.D. (登録日: 2010-02-05, 公開日: 2010-12-08, 最終更新日: 2024-04-03)

主引用文献

Daugherty, M.D.,Liu, B.,Frankel, A.D.
Structural basis for cooperative RNA binding and export complex assembly by HIV Rev.
Nat.Struct.Mol.Biol., 17:1337-1342, 2010

PubMed Abstract: HIV replication requires nuclear export of unspliced viral RNAs to translate structural proteins and package genomic RNA. Export is mediated by cooperative binding of the Rev protein to the Rev response element (RRE) RNA, to form a highly specific oligomeric ribonucleoprotein (RNP) that binds to the Crm1 host export factor. To understand how protein oligomerization generates cooperativity and specificity for RRE binding, we solved the crystal structure of a Rev dimer at 2.5-Å resolution. The dimer arrangement organizes arginine-rich helices at the ends of a V-shaped assembly to bind adjacent RNA sites and structurally couple dimerization and RNA recognition. A second protein-protein interface arranges higher-order Rev oligomers to act as an adaptor to the host export machinery, with viral RNA bound to one face and Crm1 to another, the oligomers thereby using small, interconnected modules to physically arrange the RNP for efficient export.

PubMed: 20953181
DOI: 10.1038/nsmb.1902

実験手法

X-RAY DIFFRACTION (2.5 Å)