Contrasting IgG structures reveal extreme asymmetry and flexibility

被引：193

作者：

Saphire, EO

Stanfield, RL

Crispin, MDM

Parren, PWHI

Rudd, PM

Dwek, RA

Burton, DR

Wilson, IA

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[2] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England

[3] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA

[4] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 319卷 / 01期

基金：

美国国家卫生研究院;

关键词：

intact antibody; antibody structure; IgG; hinge region; immune recognition;

D O I：

10.1016/S0022-2836(02)00244-9

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：

The crystal structure of IgG1 b12 represents the first visualization of an intact human IgG with a full-length hinge that has all domains ordered and visible. In comparison to intact murine antibodies and hinge-deletant human antibodies, b12 reveals extreme asymmetry, indicative of the extraordinary interdomain flexibility within an antibody. In addition, the structure provides an illustration of the human IgG1 hinge in its entirety and of asymmetry in the composition of the carbohydrate attached to each C,,2 domain of the Fc. The two separate hinges assume different conformations in order to accommodate the vastly different placements of the two Fab domains relative to the Fc domain. Interestingly, only one of two possible intra-hinge disulfides is formed. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：9 / 18

页数：10

共 56 条

[1] Standard conformations for the canonical structures of immunoglobulins [J].