Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution

Daniel J. Leahy, Richard Axel, Wayne A. Hendrickson

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)1145-1162
Number of pages18
JournalCell
Volume68
Issue number6
DOIs
StatePublished - Mar 20 1992

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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