3MJ9

Crystal structure of JAML in complex with the stimulatory antibody HL4E10

3MJ9 の概要

• エントリーDOI: 10.2210/pdb3mj9/pdb
• 関連するPDBエントリー: 3MJ6 3MJ7
• 分子名称: Junctional adhesion molecule-like, STIMULATORY HAMSTER ANTIBODY HL4E10 FAB LIGHT CHAIN, STIMULATORY HAMSTER ANTIBODY HL4E10 FAB HEAVY CHAIN, ... (5 entities in total)
• 機能のキーワード: immunoglobulin tandem domain, receptor-antibody complex, cell adhesion, cell junction, glycoprotein, immunoglobulin domain, membrane, costimulation, hamster igg, transmembrane, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cell junction (By similarity): Q80UL9
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 78584.56

構造登録者

Verdino, P.,Wilson, I.A. (登録日: 2010-04-12, 公開日: 2011-02-23, 最終更新日: 2024-11-27)

主引用文献

Verdino, P.,Witherden, D.A.,Ferguson, M.S.,Corper, A.L.,Schiefner, A.,Havran, W.L.,Wilson, I.A.
Molecular insights into gamma delta T cell costimulation by an anti-JAML antibody.
Structure, 19:80-89, 2011

PubMed Abstract: γδ T cells bridge innate and adaptive immunity and function in immunosurveillance, immunoregulation, tumor cell recognition, and as first line of defense against microbial infection. Costimulation of epithelial γδ T cell activation by the JAML receptor can be induced by interaction with its endogenous ligand CAR or by binding of the stimulatory antibody HL4E10. We, therefore, determined the crystal structure of the JAML-HL4E10 Fab complex at 2.95 Å resolution. HL4E10 binds the membrane-proximal domain of JAML through hydrophobic interactions that account for nanomolar affinity and long half-life, contrasting with the fast kinetics and micromolar affinity of the hydrophilic CAR interaction with the membrane-distal JAML domain. Thus, despite different binding sites and mechanisms, JAML interaction with these two disparate ligands leads to the same functional outcome, namely JAML triggering and induction of cell signaling. Several characteristics of the HL4E10 antibody might then be harnessed in therapeutic applications, such as promoting healing of acute or chronic wounds.

PubMed: 21220118
DOI: 10.1016/j.str.2010.10.007

実験手法

X-RAY DIFFRACTION (2.95 Å)