1b3j: Difference between revisions
New page: left|200px<br /> <applet load="1b3j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b3j, resolution 3.00Å" /> '''STRUCTURE OF THE MH... |
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[[Image:1b3j.gif|left|200px]]<br /> | [[Image:1b3j.gif|left|200px]]<br /><applet load="1b3j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1b3j, resolution 3.00Å" /> | caption="1b3j, resolution 3.00Å" /> | ||
'''STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND'''<br /> | '''STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND'''<br /> | ||
==Overview== | ==Overview== | ||
The major histocompatibility complex (MHC) class I homolog MIC-A functions | The major histocompatibility complex (MHC) class I homolog MIC-A functions as a stress-inducible antigen that is recognized by a subset of gammadelta T cells independent of beta2-microglobulin and bound peptides. Its crystal structure reveals a dramatically altered MHC class I fold, both in detail and overall domain organization. The only remnant of a peptide-binding groove is a small cavity formed as the result of disordering a large section of one of the groove-defining helices. Loss of beta2-microglobulin binding is due to a restructuring of the interaction interfaces. Structural mapping of sequence variation suggests potential receptor binding sites on the underside of the platform on the side opposite of the surface recognized by alphabeta T cell receptors on MHC class I-peptide complexes. | ||
==About this Structure== | ==About this Structure== | ||
1B3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1B3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: t-cell]] | [[Category: t-cell]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:07 2008'' | ||
Revision as of 12:51, 21 February 2008
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STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND
OverviewOverview
The major histocompatibility complex (MHC) class I homolog MIC-A functions as a stress-inducible antigen that is recognized by a subset of gammadelta T cells independent of beta2-microglobulin and bound peptides. Its crystal structure reveals a dramatically altered MHC class I fold, both in detail and overall domain organization. The only remnant of a peptide-binding groove is a small cavity formed as the result of disordering a large section of one of the groove-defining helices. Loss of beta2-microglobulin binding is due to a restructuring of the interaction interfaces. Structural mapping of sequence variation suggests potential receptor binding sites on the underside of the platform on the side opposite of the surface recognized by alphabeta T cell receptors on MHC class I-peptide complexes.
About this StructureAbout this Structure
1B3J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand., Li P, Willie ST, Bauer S, Morris DL, Spies T, Strong RK, Immunity. 1999 May;10(5):577-84. PMID:10367903
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