LENGTH DISTRIBUTION OF CDRH3 IN ANTIBODIES

被引：268

作者：

WU, TT

JOHNSON, G

KABAT, EA

机构：

[1] COLUMBIA UNIV COLL PHYS & SURG,DEPT MICROBIOL,NEW YORK,NY 10032

[2] COLUMBIA UNIV COLL PHYS & SURG,DEPT GENET & DEV,NEW YORK,NY 10032

[3] COLUMBIA UNIV COLL PHYS & SURG,DEPT NEUROL,NEW YORK,NY 10032

[4] NORTHWESTERN UNIV,DEPT BIOCHEM,EVANSTON,IL 60208

[5] NORTHWESTERN UNIV,DEPT MOLEC BIOL & CELL BIOL,EVANSTON,IL 60208

[6] NORTHWESTERN UNIV,DEPT ENGN SCI & APPL MATH,EVANSTON,IL 60208

[7] NORTHWESTERN UNIV,DEPT BIOMED ENGN,EVANSTON,IL 60208

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1993年 / 16卷 / 01期

关键词：

HEAVY CHAINS; COMPLEMENTARITY DETERMINING REGION; ANTIBODY SPECIFICITY; AMINO ACID LOOPS; V-(D)-J JOINING;

D O I：

10.1002/prot.340160102

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：

Sequences of the third complementarity determining region of antibody heavy chains (CDRH3s) are listed according to their length. Human sequences vary from 2 to 26 amino acids residues, but less extensively in other species. When combined with the other five complementarity determining regions, this enormous length variation of CDRH3, together with amino acid substitutions in their sequences, can provide a very large number of antibody specificities and can influence the shape of antibody combining sites.

引用

页码：1 / 7

页数：7

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[1] A STRONG PROPENSITY TOWARD LOOP FORMATION CHARACTERIZES THE EXPRESSED READING FRAMES OF THE D-SEGMENTS AT THE IG H AND T-CELL RECEPTOR LOCI [J].