1c16
From Proteopedia
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'''CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22''' | '''CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22''' | ||
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[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: Wingren, C.]] | [[Category: Wingren, C.]] | ||
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| - | [[Category: | + | [[Category: Major histocompatibility]] |
| - | [[Category: | + | [[Category: Non-classical mhc-like]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:12:32 2008'' | |
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Revision as of 09:12, 2 May 2008
CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22
Overview
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.
About this Structure
1C16 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold., Wingren C, Crowley MP, Degano M, Chien Y, Wilson IA, Science. 2000 Jan 14;287(5451):310-4. PMID:10634787 Page seeded by OCA on Fri May 2 12:12:32 2008
