Shirai H, Kidera A, Nakamura H
Department of Bioinformatics, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
FEBS Lett. 1999 Jul 16;455(1-2):188-97. doi: 10.1016/s0014-5793(99)00821-2.
For the third complementarity determining region of the antibody heavy chain (CDR-H3), we propose the 'H3-rules', which should identify the tertiary structure from the amino acid sequence of the CDR-H3 segment. A total of 100 CDR-H3 segments from well-determined crystal structures were analyzed. Distinctive relationships between the structures and the sequences were revealed from 55 segments, and the rules were examined for the other 45 segments and were verified. In some antibodies, basic residues at specific positions were revealed to be notable signals, with their ability to form salt bridges and to assume conformations inconsistent with the rules.
对于抗体重链的第三个互补决定区（CDR-H3），我们提出了“H3规则”，该规则应能从CDR-H3片段的氨基酸序列确定其三级结构。我们分析了来自已明确解析晶体结构的总共100个CDR-H3片段。从55个片段中揭示了结构与序列之间的独特关系，并对另外45个片段的规则进行了检验和验证。在一些抗体中，特定位置的碱性残基被证明是显著信号，它们能够形成盐桥并呈现与规则不一致的构象。
