Ippolito J A, Steitz T A
Department of Molecular Biophysics and Biochemistry,, New Haven, CT 06520-8114, USA.
Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9819-24. doi: 10.1073/pnas.95.17.9819.
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.
已确定包含反式激活蛋白Tat结合位点的HIV-1反式激活应答区域(TAR)RNA片段的晶体结构,分辨率达到1.3埃。在该晶体结构中,TAR特有的UCU凸起采用了一种由三个二价钙离子稳定的构象,与之前通过溶液核磁共振确定的构象不同。一个对环构象至关重要的金属离子直接与环区域的三个磷酸基团结合。该结构强调了金属离子结合对RNA结构的影响,鉴于细胞中二价金属离子的丰富性,这就提出了一个问题,即金属离子在体内是否在TAR RNA的构象以及TAR与Tat和细胞周期蛋白T的相互作用中发挥作用。