Solution structure of the N-terminal zinc binding domain of HIV-1 integrase
Solution structure of the N-terminal zinc binding domain of HIV-1 integrase
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DOI：
10.1038/nsb0797-567
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发表时间：
1997-07-01
期刊：
影响因子：
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通讯作者：
Gronenborn, AM
中科院分区：
文献类型：
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作者：
Cai, ML;Zheng, RL;Gronenborn, AM
用核磁共振波谱分析了HIV-1整合酶N-末端锌结合结构域(残基1-55；IN1-55)的溶液结构。In 1-55是二聚体，每个单体由四个螺旋组成，锌四面体与His 12，His 16，Cys 40和Cys 43配位。In 1-55以两种相互转化的构象状态存在，这两种状态在两个组氨酸侧链对锌的配位方面不同。不同的组氨酸排列与协调组氨酸周围的多肽骨架(残基9-18)的巨大构象差异有关。二聚体界面是以疏水为主的，由螺旋1的N端以及螺旋3和4的堆积形成。单体折叠与一些螺旋DNA结合蛋白的折叠非常相似，这些蛋白质含有一个螺旋-转角螺旋(HTH)基序，其中IN1-55的螺旋2和3对应于HTH基序。与DNA结合蛋白不同的是，在DNA结合蛋白中，HTH基序的第二个螺旋用于DNA识别，IN1-55使用这个螺旋进行二聚化。
The solution structure of the N-terminal zinc binding domain (residues 1-55; IN1-55) of HIV-1 integrase has been solved by NMR spectroscopy. IN1-55 is dimeric, and each monomer comprises four helices with the zinc tetrahedrally coordinated to His 12, His 16, Cys 40 and Cys 43. IN1-55 exists in two interconverting conformational states that differ with regard to the coordination of the two histidine side chains to zinc. The different histidine arrangements are associated with large conformational differences in the polypeptide backbone (residues 9-18) around the coordinating histidines. The dimer interface is predominantly hydrophobic and is formed by the packing of the N-terminal end of helix 1, and helices 3 and 4. The monomer fold is remarkably similar to that of a number of helical DNA binding proteins containing a helix-turn-helix (HTH) motif with helices 2 and 3 of IN1-55 corresponding to the HTH motif. In contrast to the DNA binding proteins where the second helix of the HTH motif is employed for DNA recognition, IN1-55 uses this helix for dimerization.