Dwek R A, Wain-Hobson S, Dower S, Gettins P, Sutton B, Perkins S J, Givol D
Nature. 1977 Mar 3;266(5597):31-7. doi: 10.1038/266031a0.
The structure of the combining site of the DNP binding IgA mouse myeloma protein MOPC 315 has been determined by a combination of high resolution nuclear magnetic resonance, electron spin resonance, model building and chemical modifications. This approach yields that general dimensions of the site, its polarity and asymmetry features, the assignment of the DNP-contact residues and their three-dimensional coordinates.
通过高分辨率核磁共振、电子自旋共振、模型构建和化学修饰相结合的方法,已确定了结合二硝基苯酚(DNP)的IgA小鼠骨髓瘤蛋白MOPC 315结合位点的结构。该方法得出了该位点的大致尺寸、其极性和不对称特征、DNP接触残基的归属及其三维坐标。