2L34

Structure of the DAP12 transmembrane homodimer

2L34 の概要

• エントリーDOI: 10.2210/pdb2l34/pdb
• 関連するPDBエントリー: 2HAC 2K4F 2L35
• 分子名称: TYRO protein tyrosine kinase-binding protein (1 entity in total)
• 機能のキーワード: immunoreceptor, transmembrane assembly, dap12, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: O43914
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 6662.08

構造登録者

Call, M.E.,Wucherpfennig, K.W.,Chou, J.J. (登録日: 2010-09-06, 公開日: 2010-11-03, 最終更新日: 2024-10-30)

主引用文献

Call, M.E.,Wucherpfennig, K.W.,Chou, J.J.
The structural basis for intramembrane assembly of an activating immunoreceptor complex.
Nat.Immunol., 11:1023-1029, 2010

PubMed Abstract: Many receptors that activate cells of the immune system are multisubunit membrane protein complexes in which ligand recognition and signaling functions are contributed by separate protein modules. Receptors and signaling subunits assemble through contacts among basic and acidic residues in their transmembrane domains to form the functional complexes. Here we report the nuclear magnetic resonance (NMR) structure of the membrane-embedded, heterotrimeric assembly formed by association of the DAP12 signaling module with the natural killer (NK) cell-activating receptor NKG2C. The main intramembrane contact site is formed by a complex electrostatic network involving five hydrophilic transmembrane residues. Functional mutagenesis demonstrated that similar polar intramembrane motifs are also important for assembly of the NK cell-activating NKG2D-DAP10 complex and the T cell antigen receptor (TCR)-invariant signaling protein CD3 complex. This structural motif therefore lies at the core of the molecular organization of many activating immunoreceptors.

PubMed: 20890284
DOI: 10.1038/ni.1943

実験手法

SOLUTION NMR