3MJ6

Crystal structure of the gammadelta T cell costimulatory receptor Junctional Adhesion Molecule-Like Protein, JAML

Summary for 3MJ6

• Entry DOI: 10.2210/pdb3mj6/pdb
• Related: 3MJ7 3MJ8 3MJ9
• Descriptor: Junctional adhesion molecule-like, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: immunoglobulin tandem domain, cell adhesion, cell junction, glycoprotein, immunoglobulin domain, membrane, costimulation, transmembrane, immune system
• Biological source: Mus musculus (mouse)
• Cellular location: Cell junction (By similarity): Q80UL9
• Total number of polymer chains: 1
• Total formula weight: 31848.34

Authors

Verdino, P.,Wilson, I.A. (deposition date: 2010-04-12, release date: 2010-09-22, Last modification date: 2024-10-09)

Primary citation

Verdino, P.,Witherden, D.A.,Havran, W.L.,Wilson, I.A.
The molecular interaction of CAR and JAML recruits the central cell signal transducer PI3K.
Science, 329:1210-1214, 2010

PubMed Abstract: Coxsackie and adenovirus receptor (CAR) is the primary cellular receptor for group B coxsackieviruses and most adenovirus serotypes and plays a crucial role in adenoviral gene therapy. Recent discovery of the interaction between junctional adhesion molecule-like protein (JAML) and CAR uncovered important functional roles in immunity, inflammation, and tissue homeostasis. Crystal structures of JAML ectodomain (2.2 angstroms) and its complex with CAR (2.8 angstroms) reveal an unusual immunoglobulin-domain assembly for JAML and a charged interface that confers high specificity. Biochemical and mutagenesis studies illustrate how CAR-mediated clustering of JAML recruits phosphoinositide 3-kinase (P13K) to a JAML intracellular sequence motif as delineated for the alphabeta T cell costimulatory receptor CD28. Thus, CAR and JAML are cell signaling receptors of the immune system with implications for asthma, cancer, and chronic nonhealing wounds.

PubMed: 20813955
DOI: 10.1126/science.1187996

Experimental method

X-RAY DIFFRACTION (2.19 Å)