Crystal Structure of a [Gamma][Delta] T Cell Receptor Ligand T22: A Truncated MHC-Like Fold

Crystal Structure of a [Gamma][Delta] T Cell Receptor Ligand T22: A Truncated MHC-Like Fold

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 on...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) Vol. 287; no. 5451; p. 310
Main Authors: Wingren, Christer, Crowley, Michael P, Degano, Massimo, Chien, Yueh-hsiu, Wilson, Ian A
Format: Journal Article
Language:English
Published: Washington American Association for the Advancement of Science 14-01-2000
The American Association for the Advancement of Science
Subjects:
Cells
Cellular biology
Crystals
Immune system
Molecules
Scientific Concepts
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ISSN:0036-8075
1095-9203