Structural classification of CDR-H3 in antibodies

被引：139

作者：

Shirai, H ^{[1
]}

Kidera, A ^{[1
]}

Nakamura, H ^{[1
]}

机构：

[1] BIOMOL ENGN RES INST,DEPT BIOINFORMAT,SUITA,OSAKA 565,JAPAN

来源：

FEBS LETTERS | 1996年 / 399卷 / 1-2期

关键词：

antibody; complementarity determining region; loop modeling; structure classification;

D O I：

10.1016/S0014-5793(96)01252-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 ,veil 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.

引用

页码：1 / 8

页数：8

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