3OMZ

Crystal structure of MICA-specific human gamma delta T cell receptor

Summary for 3OMZ

• Entry DOI: 10.2210/pdb3omz/pdb
• Descriptor: human Vdelta1 gamma delta T cell receptor delta1A/B-3 (1 entity in total)
• Functional Keywords: immunoglobulin fold, immune surveillance of cell stress protein mic-a/b, mic-a/b binding, epithelium, immune system
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 116931.76

Authors

Xu, B.,Holmes, M.A.,Strong, R.K. (deposition date: 2010-08-27, release date: 2011-01-26, Last modification date: 2024-10-09)

Primary citation

Xu, B.,Pizarro, J.C.,Holmes, M.A.,McBeth, C.,Groh, V.,Spies, T.,Strong, R.K.
Crystal structure of a {gamma}{delta} T-cell receptor specific for the human MHC class I homolog MICA.
Proc.Natl.Acad.Sci.USA, 108:2414-2419, 2011

PubMed Abstract: γδ T cells play important roles in bridging innate and adaptive immunity, but their recognition mechanisms remain poorly understood. Human γδ T cells of the V(δ)1 subset predominate in intestinal epithelia and respond to MICA and MICB (MHC class I chain-related, A and B; MIC) self-antigens, mediating responses to tumorigenesis or viral infection. The crystal structure of an MIC-reactive V(δ)1 γδ T-cell receptor (TCR) showed expected overall structural homology to antibodies, αβ, and other γδ TCRs, but complementary determining region conformations and conservation of V(δ)1 use revealed an uncharacteristically flat potential binding surface. MIC, likewise, serves as a ligand for the activating immunoreceptor natural killer group 2, D (NKG2D), also expressed on γδ T cells. Although MIC recognition drives both the TCR-dependent stimulatory and NKG2D-dependent costimulatory signals necessary for activation, interaction analyses showed that MIC binding by the two receptors was mutually exclusive. Analysis of relative binding kinetics suggested sequential recognition, defining constraints for the temporal organization of γδ T-cell/target cell interfaces.

PubMed: 21262824
DOI: 10.1073/pnas.1015433108

Experimental method

X-RAY DIFFRACTION (3.04 Å)