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TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes...
Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55Å resolution. The binary complex forms a characteristic “V” shape for substrate binding and contains the four motifs conserved in...
The structure of the I domain of integrin αLβ2 bound to the Ig superfamily ligand ICAM-1 reveals the open ligand binding conformation and the first example of an integrin-IgSF interface. The I domain Mg 2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. Liganded and unliganded structures for both high- and intermediate-affinity...
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