Structural classification of CDR‐H3 in antibodies

FEBS Letters

Nakamura, Haruki¹  Shirai, Hiroki¹  Kidera, Akinori¹ 

[1] Department of Bioinformatics, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan

关键词: Antibody;    Complementarity determining region;    Loop modeling;    Structure classification;    CDR;    complementarity determining region;    3D;    three-dimensional;   

DOI  :  10.1016/S0014-5793(96)01252-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown