STRUCTURE OF HIV-1 RT/TIBO R-86183 COMPLEX REVEALS SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE INHIBITORS
STRUCTURE OF HIV-1 RT/TIBO R-86183 COMPLEX REVEALS SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE INHIBITORS
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DOI：
10.1038/nsb0595-407
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发表时间：
1995-05-01
期刊：
影响因子：
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通讯作者：
ARNOLD, E
中科院分区：
文献类型：
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作者：
DING, JP;DAS, K;ARNOLD, E
我们报告了HIV-1逆转录酶（RT）与非核苷抑制剂TIBO R 86183复合的3.0埃分辨率的结构。将该结构与HIV-1 RT/α-APA R 95845和HIV-1 RT/奈韦拉平复合物的结构进行比较，为理解非核苷抑制剂结合的性质、结合位点的结构和结合的抑制剂与周围氨基酸残基之间的相互作用以及理解非核苷抑制剂的抑制和耐药性机制提供了基础。所考虑的所有三种抑制剂都呈现类似的蝴蝶状形状，并以非常相似的方式与HIV-1 RT结合。形成结合口袋的氨基酸残基的构象存在重要差异。
We report the structure of HIV-I reverse transcriptase (RT) complexed with the nonnucleoside inhibitor TIBO R 86183 at 3.0 Angstrom resolution. Comparing this structure with those of complexes of HIV-1 RT/alpha-APA R 95845 and HIV-1 RT/nevirapine provides a basis for understanding the nature of nonnucleoside inhibitor binding, the structure of the binding site and the interactions between the bound inhibitors and surrounding amino acid residues as well as for understanding mechanisms of inhibition by and resistance to nonnucleoside inhibitors. Ail three inhibitors considered assume a similar butterfly-like shape and bind to HIV-1 RT in a very similar way. important differences occur in the conformation of amino acid residues that form the binding pocket.