Cai M, Huang Y, Caffrey M, Zheng R, Craigie R, Clore G M, Gronenborn A M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Protein Sci. 1998 Dec;7(12):2669-74. doi: 10.1002/pro.5560071221.
The solution structure of His12 --> Cys mutant of the N-terminal zinc binding domain (residues 1-55; IN(1-55)) of HIV-1 integrase complexed to cadmium has been solved by multidimensional heteronuclear NMR spectroscopy. The overall structure is very similar to that of the wild-type N-terminal domain complexed to zinc. In contrast to the wild-type domain, however, which exists in two interconverting conformational states arising from different modes of coordination of the two histidine side chains to the metal, the cadmium complex of the His12 --> Cys mutant exists in only a single form at low pH. The conformation of the polypeptide chain encompassing residues 10-18 is intermediate between the two forms of the wild-type complex.
通过多维异核核磁共振光谱法解析了与镉结合的HIV-1整合酶N端锌结合结构域(第1至55位残基;IN(1-55))的His12→Cys突变体的溶液结构。其整体结构与与锌结合的野生型N端结构域非常相似。然而,与野生型结构域不同,野生型结构域由于两个组氨酸侧链与金属的不同配位模式而存在两种相互转化的构象状态,His12→Cys突变体的镉配合物在低pH下仅以单一形式存在。包含第10至18位残基的多肽链构象处于野生型配合物两种形式之间的中间状态。