2HAC

Structure of Zeta-Zeta Transmembrane Dimer

Summary for 2HAC

• Entry DOI: 10.2210/pdb2hac/pdb
• Descriptor: T-cell surface glycoprotein CD3 zeta chain (1 entity in total)
• Functional Keywords: transmembrane, alpha helix, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P20963
• Total number of polymer chains: 2
• Total formula weight: 7510.95

Authors

Chou, J.J.,Wucherpfennig, K.W.,Schnell, J.R.,Call, M.E. (deposition date: 2006-06-12, release date: 2006-10-31, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

SOLUTION NMR