3DJ9

Crystal Structure of an isolated, unglycosylated antibody CH2 domain

3DJ9 の概要

• エントリーDOI: 10.2210/pdb3dj9/pdb
• 関連するPDBエントリー: 1HZH 1OQO 2DTQ 2DTS
• 分子名称: Ig gamma-1 chain C region (2 entities in total)
• 機能のキーワード: antibody, immunoglobulin, ch2 domain, glycoprotein, immunoglobulin c region, immunoglobulin domain, secreted, immune system
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted: P01857
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12087.82

構造登録者

Prabakaran, P.,Vu, B.K.,Gan, J.,Dimitrov, D.S.,Ji, X. (登録日: 2008-06-22, 公開日: 2008-09-16, 最終更新日: 2024-10-30)

主引用文献

Prabakaran, P.,Vu, B.K.,Gan, J.,Feng, Y.,Dimitrov, D.S.,Ji, X.
Structure of an isolated unglycosylated antibody C(H)2 domain.
Acta Crystallogr.,Sect.D, 64:1062-1067, 2008

PubMed Abstract: The C(H)2 (C(H)3 for IgM and IgE) domain of an antibody plays an important role in mediating effector functions and preserving antibody stability. It is the only domain in human immunoglobulins (Igs) which is involved in weak interchain protein-protein interactions with another C(H)2 domain solely through sugar moieties. The N-linked glycosylation at Asn297 is conserved in mammalian IgGs as well as in homologous regions of other antibody isotypes. To examine the structural details of the C(H)2 domain in the absence of glycosylation and other antibody domains, the crystal structure of an isolated unglycosylated antibody gamma1 C(H)2 domain was determined at 1.7 A resolution and compared with corresponding C(H)2 structures from intact Fc, IgG and Fc receptor complexes. Furthermore, the oligomeric state of the protein in solution was studied using size-exclusion chromatography. The results suggested that the unglycosylated human antibody C(H)2 domain is a monomer and that its structure is similar to that found in the intact Fc, IgG and Fc receptor complex structures. However, certain structural variations were observed in the Fc receptor-binding sites. Owing to its small size, stability and non-immunogenic Ig template, the C(H)2-domain structure could be useful for the development by protein design of antibody domains exerting effector functions and/or antigen specificity and as a robust scaffold in protein-engineering applications.

PubMed: 18931413
DOI: 10.1107/S0907444908025274

実験手法

X-RAY DIFFRACTION (1.75 Å)