1bqh

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(New page: 200px<br /><applet load="1bqh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqh, resolution 2.8&Aring;" /> '''MURINE CD8AA ECTODOMA...)
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[[Image:1bqh.gif|left|200px]]<br /><applet load="1bqh" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bqh.gif|left|200px]]<br /><applet load="1bqh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bqh, resolution 2.8&Aring;" />
caption="1bqh, resolution 2.8&Aring;" />
'''MURINE CD8AA ECTODOMAIN FRAGMENT IN COMPLEX WITH H-2KB/VSV8'''<br />
'''MURINE CD8AA ECTODOMAIN FRAGMENT IN COMPLEX WITH H-2KB/VSV8'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1BQH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NDG and NAG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BQH OCA].
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1BQH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQH OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Chang, H.C.]]
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[[Category: Chang, H C.]]
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[[Category: Kern, P.S.]]
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[[Category: Kern, P S.]]
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[[Category: Reinherz, E.L.]]
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[[Category: Reinherz, E L.]]
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[[Category: Wang, J.H.]]
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[[Category: Wang, J H.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: NDG]]
[[Category: NDG]]
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[[Category: t-cell]]
[[Category: t-cell]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:50:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:00 2008''

Revision as of 09:58, 21 February 2008

Image:1bqh.gif

1bqh, resolution 2.8Å

Drag the structure with the mouse to rotate

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 with and as ligands. 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 Thu Feb 21 11:58:00 2008

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