1SY6

Crystal Structure of CD3gammaepsilon Heterodimer in Complex with OKT3 Fab Fragment

Summary for 1SY6

• Entry DOI: 10.2210/pdb1sy6/pdb
• Descriptor: OKT3 Fab light chain, OKT3 Fab heavy chain, T-cell surface glycoprotein CD3 gamma/epsilon chain (3 entities in total)
• Functional Keywords: cd3 gamma, cd3 epsilon, okt3 fab, signaling protein-antibiotic complex, signaling protein/antibiotic
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane ; Single-pass type I membrane protein : P07766
• Total number of polymer chains: 3
• Total formula weight: 70159.85

Authors

Kjer-Nielsen, L.,Dunstone, M.A.,Kostenko, L.,Ely, L.K.,Beddoe, T.,Misfud, N.A.,Purcell, A.W.,Brooks, A.G.,McCluskey, J.,Rossjohn, J. (deposition date: 2004-03-31, release date: 2004-05-25, Last modification date: 2024-10-30)

Primary citation

Kjer-Nielsen, L.,Dunstone, M.A.,Kostenko, L.,Ely, L.K.,Beddoe, T.,Mifsud, N.A.,Purcell, A.W.,Brooks, A.G.,McCluskey, J.,Rossjohn, J.
Crystal structure of the human T cell receptor CD3(epsilon)(gamma) heterodimer complexed to the therapeutic mAb OKT3.
Proc.Natl.Acad.Sci.USA, 101:7675-7680, 2004

PubMed Abstract: The CD3 epsilon gamma heterodimer is essential for expression and function of the T cell receptor. The crystal structure of the human CD3 epsilon gamma heterodimer is described to 2.1-A resolution complexed with OKT3, a therapeutic mAb that not only activates and tolerizes mature T cells but also induces regulatory T cells. The mode of CD3 epsilon gamma dimerization provides a general structural basis for CD3 assembly and maps candidate T cell antigen receptor docking sites, including a duplicated linear region rich in acidic residues that is unique to human CD3 epsilon. OKT3 binds to an atypically small area of CD3 epsilon and has a low affinity for the isolated CD3 epsilon gamma heterodimer. The structure of the OKT3/CD3 epsilon gamma complex has implications for T cell signaling and therapeutic design.

PubMed: 15136729
DOI: 10.1073/pnas.0402295101

Experimental method

X-RAY DIFFRACTION (2.1 Å)