Matsugami Akimasa, Tamura Yusuke, Kudo Michiko, Uesugi Seiichi, Yamamoto Rika, Kumar Penmetcha, Katahira Masato
Department of Environment and Natural Sciences, Graduate School of Environment and Information Sciences, Yokohama National University, 79-7 Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan.
Nucleic Acids Symp Ser (Oxf). 2004(48):111-2. doi: 10.1093/nass/48.1.111.
An RNA aptamer containing two binding sites exhibits extremely high affinity to the HIV Tat protein. We previously reported the structure of the aptamer complexed with argininamide as the simplest analogue of Tat. Here, we have analyzed the structure of the aptamer complexed with the partial peptide of Tat, RKKRR. The profile of chemical sift perturbations for the aptamer upon complex formation with RKKRR revealed that RKKRR can be a realistic analogue of Tat to address the interactions between the arginine-rich motif of Tat and the aptamer. It was suggested that the aptamer interacts with different arginine residues of RKKRR simultaneously at the two binding sites, which can explain the extremely high affinity to Tat.
一种含有两个结合位点的RNA适配体对HIV Tat蛋白表现出极高的亲和力。我们之前报道了该适配体与精氨酰胺（作为Tat的最简单类似物）复合后的结构。在此，我们分析了该适配体与Tat的部分肽段RKKRR复合后的结构。与RKKRR复合时适配体的化学位移扰动图谱显示，RKKRR可以作为Tat的一个现实类似物来研究Tat富含精氨酸基序与适配体之间的相互作用。研究表明，该适配体在两个结合位点同时与RKKRR的不同精氨酸残基相互作用，这可以解释其对Tat的极高亲和力。
