 |
PDBsum entry 1bqh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
1bqh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
274 a.a.
|
|
|
|
|
|
|
|
|
|
|
99 a.a.
|
|
|
|
|
|
|
|
|
|
|
122 a.a.
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis of cd8 coreceptor function revealed by crystallographic analysis of a murine cd8alphaalpha ectodomain fragment in complex with h-2kb.
|
|
|
Authors
|
|
P.S.Kern,
M.K.Teng,
A.Smolyar,
J.H.Liu,
J.Liu,
R.E.Hussey,
R.Spoerl,
H.C.Chang,
E.L.Reinherz,
J.H.Wang.
|
|
|
Ref.
|
|
Immunity, 1998,
9,
519-530.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Overall View of the m-CD8aa/
VSV8-H-2K
b
Crystal Structure
|
|
Figure 5.
Figure 5. Detailed Interaction among mCD8aa and H-2K
b
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Immunity
(1998,
9,
519-530)
copyright 1998.
|
|
|
|
|
|
|
