Klemba M, Gardner K H, Marino S, Clarke N D, Regan L
Department of Molecular Biophysics & Biochemistry Yale University, New Haven, Connecticut 06520, USA.
Nat Struct Biol. 1995 May;2(5):368-73. doi: 10.1038/nsb0595-368.
We describe the successful design of a tetrahedral His3Cys Zn(II)-binding site in a small protein of known structure: the B1 domain of Streptococcal protein G. The B1 variants containing the novel metal-binding site were characterized using a combination of optical absorption, circular dichroism and NMR spectroscopies. The results indicate that the designed proteins bind Zn(II) with high affinity and tetrahedral coordination geometry, and that the overall secondary and tertiary structure of the B1 domain is maintained.
我们描述了在已知结构的小蛋白质——链球菌蛋白G的B1结构域中成功设计出一个四面体His3Cys锌（II）结合位点。使用光吸收、圆二色性和核磁共振光谱相结合的方法对含有新型金属结合位点的B1变体进行了表征。结果表明，设计的蛋白质以高亲和力和四面体配位几何结构结合锌（II），并且B1结构域的整体二级和三级结构得以维持。
