3MJ7: Crystal Structure Of The Complex Of Jaml And Coxsackie And Adenovirus Receptor, Car

Citation:
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.
PDB ID: 3MJ7Download
MMDB ID: 85032
PDB Deposition Date: 2010/4/12
Updated in MMDB: 2010/09
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3MJ7: dimeric; determined by author and by software (PISA)
Molecular Components in 3MJ7
Label Count Molecule
Proteins (2 molecules)
1
Junctional Adhesion Molecule-like(Gene symbol: Jaml)
Molecule annotation
1
Coxsackievirus and Adenovirus Receptor Homolog(Gene symbol: Cxadr)
Molecule annotation
Chemicals (8 molecules)
1
5
2
1
3
1
4
1
* Click molecule labels to explore molecular sequence information.

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