2HAC

Structure of Zeta-Zeta Transmembrane Dimer

2HAC の概要

• エントリーDOI: 10.2210/pdb2hac/pdb
• 分子名称: T-cell surface glycoprotein CD3 zeta chain (1 entity in total)
• 機能のキーワード: transmembrane, alpha helix, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P20963
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7510.95

構造登録者

Chou, J.J.,Wucherpfennig, K.W.,Schnell, J.R.,Call, M.E. (登録日: 2006-06-12, 公開日: 2006-10-31, 最終更新日: 2024-11-20)

主引用文献

Call, M.E.,Schnell, J.R.,Xu, C.,Lutz, R.A.,Chou, J.J.,Wucherpfennig, K.W.
The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor.
Cell(Cambridge,Mass.), 127:355-368, 2006

PubMed Abstract: The T cell receptor (TCR) alphabeta heterodimer communicates ligand binding to the cell interior via noncovalently associated CD3gammaepsilon, CD3deltaepsilon, and zetazeta dimers. While structures of extracellular components of the TCR-CD3 complex are known, the transmembrane (TM) domains that mediate assembly have eluded structural characterization. Incorporation of the zetazeta signaling module is known to require one basic TCRalpha and two zetazeta aspartic acid TM residues. We report the NMR structure of the zetazeta(TM) dimer, a left-handed coiled coil with substantial polar contacts. Mutagenesis experiments demonstrate that three polar positions are critical for zetazeta dimerization and assembly with TCR. The two aspartic acids create a single structural unit at the zetazeta interface stabilized by extensive hydrogen bonding, and there is evidence for a structural water molecule (or molecules) within close proximity. This structural unit, representing only the second transmembrane dimer interface solved to date, serves as a paradigm for the assembly of all modules involved in TCR signaling.

PubMed: 17055436
DOI: 10.1016/j.cell.2006.08.044

実験手法

SOLUTION NMR