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Article

Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold.

Science (New York, N.Y.) - 14 Jan 2000

Wingren C, Crowley M P, Degano M, Chien Y, Wilson I A

Abstract excerpt

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...

Read the complete abstract on PubMed

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Share to beta 2-Microglobulin
Share to Glycosylation
Share to Histocompatibility Antigens Class I

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Protein Folding

Share to Protein Structure, Quaternary

Share to Receptors, Antigen, T-Cell, gamma-delta

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Source

Identifiers

PMID: 10634787
DOI: 10.1126/science.287.5451.310

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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