Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10.
AuthorsIdo H, Harada K, Futaki S, Hayashi Y, Nishiuchi R, Natsuka Y, Li S, Wada Y, Combs AC, Ervasti JM, Sekiguchi K,
JournalJ Biol Chem
PubMed ID14701821
'The adhesive interactions of cells with laminins are mediated by integrins and non-integrin-type receptors such as alpha-dystroglycan and syndecans. Laminins bind to these receptors at the C-terminal globular domain of their alpha chains, but the regions recognized by these receptors have not been mapped precisely. In this study, we sought ... More
Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactions.
AuthorsBradley KA, Mogridge J, Jonah G, Rainey A, Batty S, Young JA,
JournalJ Biol Chem
PubMed ID14507921
The secreted protein toxin produced by Bacillus anthracis contributes to virulence of this pathogen and can cause many of the symptoms seen during an anthrax infection, including shock and sudden death. The cell-binding component of anthrax toxin, protective antigen, mediates entry of the toxin into cells by first binding directly ... More
T cell immunoglobulin mucin-3 crystal structure reveals a galectin-9-independent ligand-binding surface.
AuthorsCao E, Zang X, Ramagopal UA, Mukhopadhaya A, Fedorov A, Fedorov E, Zencheck WD, Lary JW, Cole JL, Deng H, Xiao H, Dilorenzo TP, Allison JP, Nathenson SG, Almo SC,
JournalImmunity
PubMed ID17363302
The T cell immunoglobulin mucin (Tim) family of receptors regulates effector CD4(+) T cell functions and is implicated in autoimmune and allergic diseases. Tim-3 induces immunological tolerance, and engagement of the Tim-3 immunoglobulin variable (IgV) domain by galectin-9 is important for appropriate termination of T helper 1-immune responses. The 2 ... More