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1bqh
From Proteopedia
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|PDB= 1bqh |SIZE=350|CAPTION= <scene name='initialview01'>1bqh</scene>, resolution 2.8Å | |PDB= 1bqh |SIZE=350|CAPTION= <scene name='initialview01'>1bqh</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqh OCA], [http://www.ebi.ac.uk/pdbsum/1bqh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bqh RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Reinherz, E L.]] | [[Category: Reinherz, E L.]] | ||
[[Category: Wang, J H.]] | [[Category: Wang, J H.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: NDG]] | ||
[[Category: antigen]] | [[Category: antigen]] | ||
[[Category: complex]] | [[Category: complex]] | ||
| Line 36: | Line 37: | ||
[[Category: t-cell]] | [[Category: t-cell]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:06:07 2008'' |
Revision as of 16:06, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MURINE CD8AA ECTODOMAIN FRAGMENT IN COMPLEX WITH H-2KB/VSV8
Overview
The crystal structure of the two immunoglobulin variable-like domains of the murine CD8alphaalpha homodimer complexed to the class I MHC H-2Kb molecule at 2.8 A resolution shows that CD8alphaalpha binds to the protruding MHC alpha3 domain loop in an antibody-like manner. Comparison of mouse CD8alphaalpha/H-2Kb and human CD8alphaalpha/HLA-A2 complexes reveals shared as well as species-specific recognition features. In both species, coreceptor function apparently involves the participation of CD8 dimer in a bidentate attachment to an MHC class I molecule in conjunction with a T cell receptor without discernable conformational alteration of the peptide or MHC antigen-presenting platform.
About this Structure
1BQH is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb., Kern PS, Teng MK, Smolyar A, Liu JH, Liu J, Hussey RE, Spoerl R, Chang HC, Reinherz EL, Wang JH, Immunity. 1998 Oct;9(4):519-30. PMID:9806638
Page seeded by OCA on Sun Mar 30 19:06:07 2008
Categories: Mus musculus | Protein complex | Chang, H C. | Kern, P S. | Reinherz, E L. | Wang, J H. | Antigen | Complex | Coreceptor | Glycoprotein | Immunology | Signal | T-cell
