4K3D

Crystal structure of bovine antibody BLV1H12 with ultralong CDR H3

4K3D の概要

• エントリーDOI: 10.2210/pdb4k3d/pdb
• 関連するPDBエントリー: 4K3E
• 分子名称: BOVINE ANTIBODY WITH ULTRALONG CDR H3, HEAVY CHAIN, BOVINE ANTIBODY WITH ULTRALONG CDR H3, LIGHT CHAIN, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: immunoglobulin, cystine knot, immune recognition, immune system
• 由来する生物種: Bos taurus (bovine); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 104876.59

構造登録者

Ekiert, D.C.,Wang, F.,Wilson, I.A. (登録日: 2013-04-10, 公開日: 2013-06-19, 最終更新日: 2024-10-16)

主引用文献

Wang, F.,Ekiert, D.C.,Ahmad, I.,Yu, W.,Zhang, Y.,Bazirgan, O.,Torkamani, A.,Raudsepp, T.,Mwangi, W.,Criscitiello, M.F.,Wilson, I.A.,Schultz, P.G.,Smider, V.V.
Reshaping antibody diversity.
Cell(Cambridge,Mass.), 153:1379-1393, 2013

PubMed Abstract: Some species mount a robust antibody response despite having limited genome-encoded combinatorial diversity potential. Cows are unusual in having exceptionally long CDR H3 loops and few V regions, but the mechanism for creating diversity is not understood. Deep sequencing reveals that ultralong CDR H3s contain a remarkable complexity of cysteines, suggesting that disulfide-bonded minidomains may arise during repertoire development. Indeed, crystal structures of two cow antibodies reveal that these CDR H3s form a very unusual architecture composed of a β strand "stalk" that supports a structurally diverse, disulfide-bonded "knob" domain. Diversity arises from somatic hypermutation of an ultralong DH with a severe codon bias toward mutation to cysteine. These unusual antibodies can be elicited to recognize defined antigens through the knob domain. Thus, the bovine immune system produces an antibody repertoire composed of ultralong CDR H3s that fold into a diversity of minidomains generated through combinations of somatically generated disulfides.

PubMed: 23746848
DOI: 10.1016/j.cell.2013.04.049

実験手法

X-RAY DIFFRACTION (1.85 Å)