CONFORMATION OF THE TAR RNA-ARGININE COMPLEX BY NMR-SPECTROSCOPY
CONFORMATION OF THE TAR RNA-ARGININE COMPLEX BY NMR-SPECTROSCOPY
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DOI：
10.1126/science.1621097
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发表时间：
1992-07-03
期刊：
影响因子：
56.9
通讯作者：
WILLIAMSON, JR
中科院分区：
文献类型：
--
作者：
PUGLISI, JD;TAN, RY;WILLIAMSON, JR
人类免疫缺陷病毒-1（HIV-1）的信使RNA在其5'末端具有RNA发夹结构TAR，其含有六核苷酸环和三核苷酸凸起。TAR RNA和TAR与特异性结合在病毒蛋白达特结合位点的精氨酸类似物的构象通过核磁共振（NMR）光谱进行表征。在精氨酸结合时，凸起改变构象，并且用于结合的必需核苷酸U23和A27.U38形成碱基-三重相互作用，其稳定精氨酸与G26和磷酸的氢键。精氨酸-TAR相互作用的特异性似乎主要来源于RNA的结构。
The messenger RNAs of human immunodeficiency virus-1 (HIV-1) have an RNA hairpin structure, TAR, at their 5' ends that contains a six-nucleotide loop and a three-nucleotide bulge. The conformations of TAR RNA and of TAR with an arginine analog specifically bound at the binding site for the viral protein, Tat, were characterized by nuclear magnetic resonance (NMR) spectroscopy. Upon arginine binding, the bulge changes conformation, and essential nucleotides for binding, U23 and A27.U38, form a base-triple interaction that stabilizes arginine hydrogen bonding to G26 and phosphates. Specificity in the arginine-TAR interaction appears to be derived largely from the structure of the RNA.