2A6D

Crystal structure analysis of the anti-arsonate germline antibody 36-65 in complex with a phage display derived dodecapeptide RLLIADPPSPRE

2A6D の概要

• エントリーDOI: 10.2210/pdb2a6d/pdb
• 分子名称: Germline antibody 36-65 Fab light chain, Germline antibody 36-65 Fab Heavy chain, Dodecapeptide, RLLIADPPSPRE, ... (4 entities in total)
• 機能のキーワード: germline, fab, antibody, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 96665.21

構造登録者

Sethi, D.K.,Agarwal, A.,Manivel, V.,Rao, K.V.,Salunke, D.M. (登録日: 2005-07-02, 公開日: 2006-06-13, 最終更新日: 2024-11-13)

主引用文献

Sethi, D.K.,Agarwal, A.,Manivel, V.,Rao, K.V.,Salunke, D.M.
Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response.
Immunity, 24:429-438, 2006

PubMed Abstract: Correlation between the promiscuity of the primary antibody response and conformational flexibility in a germline antibody was addressed by using germline antibody 36-65. Crystallographic analyses of the 36-65 Fab with three independent dodecapeptides provided mechanistic insights into the generation of antibody diversity. While four antigen-free Fab molecules provided a quantitative description of the conformational repertoire of the antibody CDRs, three Fab molecules bound to structurally diverse peptide epitopes exhibited a common paratope conformation. Each peptide revealed spatially different footprints within the antigen-combining site. However, a conformation-specific lock involving two shared residues, which were also associated with hapten binding, was discernible. Unlike the hapten, the peptides interacted with residues that undergo somatic mutations, suggesting a possible mechanism for excluding "nonspecific" antigens during affinity maturation. The observed multiple binding modes of diverse epitopes within a common paratope conformation of a germline antibody reveal a simple, yet elegant, mechanism for expanding the primary antibody repertoire.

PubMed: 16618601
DOI: 10.1016/j.immuni.2006.02.010

実験手法

X-RAY DIFFRACTION (2.9 Å)