Journal
SCIENCE
Volume 301, Issue 5640, Pages 1725-1728Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1085643
Keywords
-
Categories
Funding
- NCI NIH HHS [CA080942] Funding Source: Medline
- NHLBI NIH HHS [HL61001] Funding Source: Medline
Ask authors/readers for more resources
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-LckZn(2+) 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available