Cell
Volume 68, Issue 6, 20 March 1992, Pages 1145-1162
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Article
Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution

https://doi.org/10.1016/0092-8674(92)90085-QGet rights and content

Abstract

A secreted fragment of the extracellular portion of human CD8α has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 Å resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8α are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form Fv-like homodimers.

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      As seen in a structural model of CD28 (Figure 7A), the residues that comprise the hinge domain of the CD28 homodimer span the dimerization interface and play an important role in the formation of CD28 homodimers.40 In structural studies of the CD8α homodimer, a 141-amino acid construct was expressed comprising the N-terminal 114-amino acid immunoglobulin domain and a 27-amino acid C-terminal tail.41 These studies revealed that the tail of this construct was not ordered, which suggested flexibility of this region.

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