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A recent crystal structure of the N15 ␣ր␤-T cell receptor (TCR) in complex with an Fab derived from the H57 C ␤-specific monoclonal antibody (mAb) shows the mAb fragment interacting with the elongated FG loop of the C ␤ domain. This loop creates one side wall of a cavity within the TCR Ti-␣ր␤ constant region module (C ␣ C ␤) while the CD and EF loops of the(More)
Soluble mouse CD8␣␣ and CD8␣␤ dimers corresponding to the paired ectodomains (CD8 f) or their respective component Ig-like domains (CD8) were expressed in Chinese hamster ovary cells or the glycosylation variant Lec3.2.8.1 cells as secreted proteins using a leucine zipper strategy. The affinity of CD8␣␣ f for H-2K b as measured by BIAcore revealed a ϳ65 ␮M(More)
The asymmetric disposition of T cell receptor (TCR) Cbeta and Calpha ectodomains creates a cavity with a side-wall formed by the rigid Cbeta FG loop. To investigate the significance of this conserved structure, we generated loop deletion (betaDeltaFG) and betawt transgenic (tg) mice using the TCR beta subunit of the N15 CTL. N15betawt and N15betaDeltaFG(More)
The 50-kD CD2 (T11) molecule, originally defined as the sheep erythrocyte receptor, plays an important role in T lymphocyte activation as well as in facilitating adhesion between T lymphocytes and their cognate partners (1-5). Perturbation of the ex-tracellular domain ofCD2 by its ligand, LFA-3, or certain anti-CD2 mAbs provides signals that synergize to(More)
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