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

被引：197

作者：

Kim, PW

Sun, ZYJ

Blacklow, SC

Wagner, G

Eck, MJ ^{[1
]}

机构：

[1] Dana Farber Canc Inst, Dept Canc Biol, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA

来源：

SCIENCE | 2003年 / 301卷 / 5640期

关键词：

D O I：

10.1126/science.1085643

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1725 / 1728

页数：4

共 26 条

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