1C16

CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22

Summary for 1C16

• Entry DOI: 10.2210/pdb1c16/pdb
• Descriptor: MHC-LIKE PROTEIN T22, PROTEIN (BETA-2-MICROGLOBULIN) (2 entities in total)
• Functional Keywords: non-classical mhc-like, major histocompatibility, beta2-microglobulin, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 8
• Total formula weight: 166670.73

Authors

Wingren, C.,Crowley, M.P.,Degano, M.,Chien, Y.,Wilson, I.A. (deposition date: 1999-07-20, release date: 2000-01-26, Last modification date: 2024-10-30)

Primary citation

Wingren, C.,Crowley, M.P.,Degano, M.,Chien, Y.,Wilson, I.A.
Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold.
Science, 287:310-314, 2000

PubMed Abstract: Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gammadelta T cell receptors (TCRs) in the absence of other components. The crystal structure of T22b at 3.1 angstroms reveals similarities to MHC class I molecules, but one side of the normal peptide-binding groove is severely truncated, which allows direct access to the beta-sheet floor. Potential gammadelta TCR-binding sites can be inferred from functional mapping of T10 and T22 point mutants and allelic variants. Thus, T22 represents an unusual variant of the MHC-like fold and indicates that gammadelta and alphabeta TCRs interact differently with their respective MHC ligands.

PubMed: 10634787
DOI: 10.1126/science.287.5451.310

Experimental method

X-RAY DIFFRACTION (3.1 Å)