1c16
From Proteopedia
(New page: 200px<br /> <applet load="1c16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c16, resolution 3.10Å" /> '''CRYSTAL STRUCTURE A...) |
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- | [[Image:1c16.gif|left|200px]]<br /> | + | [[Image:1c16.gif|left|200px]]<br /><applet load="1c16" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1c16" size=" | + | |
caption="1c16, resolution 3.10Å" /> | caption="1c16, resolution 3.10Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22'''<br /> | ||
==Overview== | ==Overview== | ||
- | Murine T10 and T22 are highly related nonclassical major | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1C16 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1C16 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C16 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chien, Y.]] | [[Category: Chien, Y.]] | ||
- | [[Category: Crowley, M | + | [[Category: Crowley, M P.]] |
[[Category: Degano, M.]] | [[Category: Degano, M.]] | ||
- | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: Wingren, C.]] | [[Category: Wingren, C.]] | ||
[[Category: beta2-microglobulin]] | [[Category: beta2-microglobulin]] | ||
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[[Category: non-classical mhc-like]] | [[Category: non-classical mhc-like]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:20 2008'' |
Revision as of 10:01, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T22
Contents |
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.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
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 Thu Feb 21 12:01:20 2008