Sheriff S, Jeffrey P D, Bajorath J
Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000, USA.
J Mol Biol. 1996 Nov 1;263(3):385-9. doi: 10.1006/jmbi.1996.0582.
The CH1 domains of antibodies belonging to the following five murine immunoglobulin (Ig) classes IgG1, IgG2a, IgG2b, IgG3 and IgA have been compared. The IgG CH1 domain structures are, as would be expected, similar overall, but show local conformational variations. When compared with IgG CH1 domain structures, the IgA CH1 domain displays several significant structural differences, which are a consequence of insertions/ deletions and specific structural constraints. In regions of structural differences in the IgG CH1 domains, the spatial correspondence of residues is not reflected by conventional (Kabat) sequence number. Thus the sequence alignment and numbering for CH1 domains has been revised to be consistent with the three-dimensional alignments.
已对属于以下五种小鼠免疫球蛋白(Ig)类别IgG1、IgG2a、IgG2b、IgG3和IgA的抗体的CH1结构域进行了比较。正如预期的那样,IgG的CH1结构域结构总体上相似,但存在局部构象变化。与IgG CH1结构域结构相比,IgA CH1结构域表现出几个显著的结构差异,这些差异是插入/缺失和特定结构限制的结果。在IgG CH1结构域的结构差异区域,残基的空间对应关系并未由传统的(卡巴特)序列号反映出来。因此,CH1结构域的序列比对和编号已进行修订,以与三维比对保持一致。