Crystallization and preliminary X-ray structural studies of a high-affinity CD8alphaalpha co-receptor to pMHC

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
David K ColeGeorge Fu Gao

Abstract

The class I CD8 positive T-cell response is involved in a number of conditions in which artificial down-regulation and control would be therapeutically beneficial. Such conditions include a number of autoimmune diseases and graft rejection in transplant patients. Although the CD8 T-cell response is dominated by the TCR-pMHC interaction, activation of T cells is in most cases also dependent on a number of associated signalling molecules. Previous work has demonstrated the ability of one such molecule (CD8) to act as an antagonist to T-cell activation if added in soluble form. Therefore, a high-affinity mutant CD8 (haCD8) has been developed with the aim of developing a therapeutic immunosuppressor. In order to fully understand the nature of the haCD8 interaction, this protein was crystallized using the sitting-drop vapour-diffusion method. Single haCD8 crystals were cryocooled and used for data collection. These crystals belonged to space group P6(4)22 (assumed by similarity to the wild type), with unit-cell parameters a = 101.08, c = 56.54 A. VM calculations indicated one molecule per asymmetric unit. A 2 A data set was collected and the structure is currently being determined using molecular replacement.

References

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Citations

Aug 9, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Nianzhi ZhangChun Xia
Jan 8, 2011·Protein & Cell·Ruth K MoyseyBent K Jakobsen

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