397D

A 1.3 A RESOLUTION CRYSTAL STRUCTURE OF THE HIV-1 TRANS-ACTIVATION RESPONSE REGION RNA STEM REVEALS A METAL ION-DEPENDENT BULGE CONFORMATION

397D の概要

• エントリーDOI: 10.2210/pdb397d/pdb
• 分子名称: RNA (5'-R(*GP*GP*CP*CP*AP*GP*AP*UP*CP*UP*GP*AP*GP*CP*G)-3'), RNA (5'-R(*GP*CP*UP*CP*UP*CP*UP*GP*GP*CP*CP*C)-3'), CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: double helix, overhanging bases, rna
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8747.51

構造登録者

Ippolito, J.A.,Steitz, T.A. (登録日: 1998-04-30, 公開日: 1998-09-11, 最終更新日: 2024-02-21)

主引用文献

Ippolito, J.A.,Steitz, T.A.
A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation.
Proc.Natl.Acad.Sci.USA, 95:9819-9824, 1998

PubMed Abstract: The crystal structure of an HIV-1 trans-activation response region (TAR) RNA fragment containing the binding site for the trans-activation protein Tat has been determined to 1.3-A resolution. In this crystal structure, the characteristic UCU bulge of TAR adopts a conformation that is stabilized by three divalent calcium ions and differs from those determined previously by solution NMR. One metal ion, crucial to the loop conformation, binds directly to three phosphates in the loop region. The structure emphasizes the influence of metal ion binding on RNA structure and, given the abundance of divalent metal ion in the cell, raises the question of whether metal ions play a role in the conformation of TAR RNA and the interaction of TAR with Tat and cyclin T in vivo.

PubMed: 9707559
DOI: 10.1073/pnas.95.17.9819

実験手法

X-RAY DIFFRACTION (1.3 Å)