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J Biol Chem, Vol. 273, Issue 30, 18729-18733, July 24, 1998

A Zn2+ Ion Links the Cytoplasmic Tail of CD4 and the N-terminal Region of Lck

Morgan HuseDagger §, Michael J. EckDagger parallel , and Stephen C. HarrisonDagger §parallel Dagger Dagger §§

From the Dagger  Laboratory of Molecular Medicine, Children's Hospital, § Department of Molecular and Cellular Biology, Harvard University, Departments of parallel  Biological Chemistry and Molecular Pharmacology and Dagger Dagger  Pediatrics, Harvard Medical School, and the §§ Howard Hughes Medical Institute, Boston, Massachusetts 02115

Lck is a lymphoid-specific, Src family protein-tyrosine kinase that is known to interact with the T-cell coreceptors, CD4 and CD8. This interaction, which is critical for proper T-cell function, is mediated by the N-terminal unique region of Lck and the C-terminal cytoplasmic tail of the coreceptors. A pair of cysteines on each molecule is essential for association, suggesting that CD4 or CD8 may interact with Lck by jointly coordinating a metal ion. We describe here experiments in which a maltose-binding protein fusion protein bearing the CD4 tail has been coexpressed in Escherichia coli with an N-terminal fragment of Lck. The proteins associate in the expressing cells, forming a complex that can be affinity-purified. Formation of this complex, like the in vivo interaction, depends upon the two pairs of cysteines. Biochemical and biophysical experiments show that the complex dissociates in the presence of EDTA and that it contains a single Zn2+ ion. These results are consistent with the proposal that Lck and CD4 associate by thiol-mediated co-coordination of zinc.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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