Shirai H, Kidera A, Nakamura H
Department of Bioinformatics, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
FEBS Lett. 1996 Dec 9;399(1-2):1-8. doi: 10.1016/s0014-5793(96)01252-5.
Large varieties in the lengths and the amino acid sequences of the third complementarity determining region of the antibody heavy chain (CDR-H3) have made it difficult to establish a relationship between the sequences and the tertiary structures, in contrast to the other CDRs, which are classified by their canonical structures. A total of 55 CDR-H3 segments from well determined crystal structures were analyzed, and we have derived several remarkable rules, which could partly govern the CDR-H3 conformation dependence on the sequence. Since the rules are physically reasonable, they are expected to be applicable to structural modeling and design of antibodies.
与其他根据其典型结构分类的互补决定区（CDR）不同，抗体重链第三互补决定区（CDR-H3）在长度和氨基酸序列上存在很大差异，这使得难以确定序列与三级结构之间的关系。我们分析了来自已明确晶体结构的总共55个CDR-H3片段，并得出了几条显著的规则，这些规则可以部分地决定CDR-H3构象对序列的依赖性。由于这些规则在物理上是合理的，因此有望应用于抗体的结构建模和设计。
