The molecular interaction of CAR and JAML recruits the central cell signal transducer PI3K

Science

Volumn 329, Issue 5996, 2010, Pages 1210-1214

  Verdino, Petra ^a   Witherden, Deborah A ^a   Havran, Wendy L ^a   Wilson, Ian A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; JUNCTIONAL ADHESION MOLECULE A; PHOSPHATIDYLINOSITOL 3 KINASE; VIRUS RECEPTOR; CELL ADHESION MOLECULE; CLMP PROTEIN, MOUSE; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR LIKE MEMBRANE PROTEIN; LIGAND; LYMPHOCYTE ANTIGEN RECEPTOR;

BIOCHEMISTRY; CRYSTAL STRUCTURE; CYTOLOGY; DISEASE TREATMENT; ENZYME ACTIVITY; GENETIC ENGINEERING; HOMEOSTASIS; IMMUNE SYSTEM; IMMUNITY; PROTEIN; VIRUS;

ADENOVIRUS; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; COXSACKIE VIRUS; CRYSTAL STRUCTURE; MOLECULAR INTERACTION; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN MOTIF; SIGNAL TRANSDUCTION; T LYMPHOCYTE; VIRAL GENE THERAPY; ANIMAL; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; CHO CELL LINE; CRICETULUS; CRYSTALLIZATION; EPITHELIUM; GLYCOSYLATION; HAMSTER; HYDROGEN BOND; IMMUNOLOGY; METABOLISM; MOUSE; PHYSICAL CHEMISTRY; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; T LYMPHOCYTE SUBPOPULATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; ANTIGENS, CD28; BINDING SITES; CELL ADHESION MOLECULES; CHO CELLS; COXSACKIE AND ADENOVIRUS RECEPTOR-LIKE MEMBRANE PROTEIN; CRICETINAE; CRICETULUS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; EPITHELIUM; GLYCOSYLATION; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIGANDS; MICE; PHOSPHATIDYLINOSITOL 3-KINASES; PHYSICOCHEMICAL PROCESSES; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA; RECEPTORS, VIRUS; SIGNAL TRANSDUCTION; T-LYMPHOCYTE SUBSETS;

EID: 77956280280     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1187996     Document Type: Article

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30. We thank A. Schiefner for help with the structure solution; S. Ferguson, H. Lindermuth, and J. Vanhasny for technical support; L. Teyton for providing cell lines; J. G. Luz, M. A. Adams-Cioaba, J. Stevens, D. A. Shore, A. L. Corper, R. L. Stanfield, and E. Ollmann Saphire for helpful discussions; and X. Dai and K. Saikatendu for assistance on synchrotron trips. We acknowledge the Advanced Light Source, Stanford Synchrotron Radiation Lightsource, and the Advanced Photon Source for use of their synchrotron facilities. This work was supported by NIH grants AI42266, CA58896 to I.A.W., and AI52257 and AI064811 to W.L.H., an Erwin-Schrödinger Fellowship of the Austrian Science Fund to P.V., and the Skaggs Institute. Atomic coordinates and structure factors for JAML and the CAR-JAML complex have been deposited in the Protein Data Bank with accession numbers 3MJ6 and 3MJ7 respectively. This is manuscript 18641-MB from The Scripps Research Institute.