1Q68

Solution structure of T-cell surface glycoprotein CD4 and Proto-oncogene tyrosine-protein kinase LCK fragments

1Q68 の概要

• エントリーDOI: 10.2210/pdb1q68/pdb
• NMR情報: BMRB: 5944
• 分子名称: T-cell surface glycoprotein CD4, Proto-oncogene tyrosine-protein kinase LCK, ZINC ION (3 entities in total)
• 機能のキーワード: peptide-peptide complex, helix-helix interaction, zinc coordination, beta hairpin, membrane protein-transferase complex, membrane protein/transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: P01730; Cytoplasm: P06239
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8058.59

構造登録者

Kim, P.W.,Sun, Z.Y.,Blacklow, S.C.,Wagner, G.,Eck, M.J. (登録日: 2003-08-12, 公開日: 2003-11-25, 最終更新日: 2024-05-22)

主引用文献

Kim, P.W.,Sun, Z.Y.,Blacklow, S.C.,Wagner, G.,Eck, M.J.
A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8.
Science, 301:1725-1728, 2003

PubMed 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.

PubMed: 14500983
DOI: 10.1126/science.1085643

実験手法

SOLUTION NMR