1b3j: Difference between revisions
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[[Image:1b3j.gif|left|200px]] | [[Image:1b3j.gif|left|200px]] | ||
'''STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND''' | {{Structure | ||
|PDB= 1b3j |SIZE=350|CAPTION= <scene name='initialview01'>1b3j</scene>, resolution 3.00Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= MICA-001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B3J is a [ | 1B3J is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10367903 10367903] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: t-cell]] | [[Category: t-cell]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:05:48 2008'' |
Revision as of 11:05, 20 March 2008
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, resolution 3.00Å | |||||||
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Gene: | MICA-001 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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