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1c16

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[[Image:1c16.gif|left|200px]]
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{{STRUCTURE_1c16| PDB=1c16 | SCENE= }}
{{STRUCTURE_1c16| PDB=1c16 | SCENE= }}
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'''CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22'''
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===CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10634787 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10634787}}
==About this Structure==
==About this Structure==
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[[Category: Major histocompatibility]]
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Revision as of 17:04, 30 June 2008

Image:1c16.png

Template:STRUCTURE 1c16

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

Template:ABSTRACT PUBMED 10634787

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 Mon Jun 30 20:04:03 2008

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