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首页> 外文期刊>Nature structural biology >SOLUTION STRUCTURE OF THE N-TERMINAL ZINC BINDING DOMAIN OF HIV-1 INTEGRASE
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SOLUTION STRUCTURE OF THE N-TERMINAL ZINC BINDING DOMAIN OF HIV-1 INTEGRASE

机译：HIV-1整合酶的N末端锌结合域的溶液结构

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摘要

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. [References: 65]
机译：HIV-1整合酶的N末端锌结合结构域（残基1-55; IN1-55）的溶液结构已经通过NMR光谱法解决。 IN1-55是二聚体，每个单体包含四个螺旋，锌的四面体与His 12，His 16，Cys 40和Cys 43配位。IN1-55存在两个相互转换的构象态，在两个组氨酸的配位方面不同锌的侧链。不同的组氨酸排列与配位组氨酸周围的多肽骨架（残基9-18）的构象差异较大有关。二聚体界面主要是疏水性的，由螺旋1，螺旋3和4的N末端的堆积形成。单体折叠与许多包含螺旋-转角螺旋的DNA结合蛋白的折叠显着相似。螺旋（HTH）主题，对应于HTH主题的IN1-55的螺旋2和3。与将HTH基序的第二个螺旋用于DNA识别的DNA结合蛋白相反，IN1-55使用此螺旋进行二聚化。 [参考：65]

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