Format

Send to

Choose Destination
Science. 2003 Sep 19;301(5640):1725-8.

A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8.

Author information

1
Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.

Abstract

The T cell coreceptors CD4 and CD8 both associate via their cytoplasmic tails with the N-terminus of the Src-family tyrosine kinase Lck. These interactions require zinc and are critical for T cell development and activation. We examined the folding and solution structures of ternary CD4-Lck-Zn2+ and CD8alpha-Lck-Zn2+ complexes. The coreceptor tails and the Lck N-terminus are unstructured in isolation but assemble in the presence of zinc to form compactly folded heterodimeric domains. The cofolded complexes have similar "zinc clasp" cores that are augmented by distinct structural elements. A dileucine motif required for clathrin-mediated endocytosis of CD4 is masked by Lck.

PMID:
14500983
DOI:
10.1126/science.1085643
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center