SOLUTION STRUCTURE OF A BOVINE IMMUNODEFICIENCY VIRUS TAT-TAR PEPTIDE-RNA COMPLEX
SOLUTION STRUCTURE OF A BOVINE IMMUNODEFICIENCY VIRUS TAT-TAR PEPTIDE-RNA COMPLEX
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DOI：
10.1126/science.270.5239.1200
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发表时间：
1995-11-17
期刊：
影响因子：
56.9
通讯作者：
FRANKEL, AD
中科院分区：
文献类型：
--
作者：
PUGLISI, JD;CHEN, L;FRANKEL, AD
牛免疫缺陷病毒（BIV）的达特蛋白结合其靶RNA TAR并激活转录。对应于BIV达特的RNA结合结构域的14个氨基酸的富含精氨酸的肽特异性结合BIV TAR，并且生物化学和体内实验已经鉴定了结合所需的氨基酸和核苷酸。现在已经通过核磁共振光谱确定了RNA-肽复合物的溶液结构。TAR与两个未堆叠的凸起核苷酸形成几乎连续的A型螺旋。该肽采用β-转角构象并位于RNA的大沟中。肽中的关键氨基酸与RNA中的碱基和磷酸之间的特异性接触是明显的。该结构与所有生物化学数据一致，并证明了蛋白质可以识别RNA的主要沟的方式。
The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding, The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with ail biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.